Bioelectrocatalytic CO2 Reduction by Redox Polymer-Wired Carbon Monoxide Dehydrogenase Gas Diffusion ElectrodesClick to copy article linkArticle link copied!
- Jana M. BeckerJana M. BeckerAnalytical Chemistry─Center for Electrochemical Sciences (CES), Faculty of Chemistry and Biochemistry, Ruhr-Universität Bochum, Universitätsstr. 150, D-44780 Bochum, GermanyMore by Jana M. Becker
- Anna LielpetereAnna LielpetereAnalytical Chemistry─Center for Electrochemical Sciences (CES), Faculty of Chemistry and Biochemistry, Ruhr-Universität Bochum, Universitätsstr. 150, D-44780 Bochum, GermanyMore by Anna Lielpetere
- Julian SzczesnyJulian SzczesnyAnalytical Chemistry─Center for Electrochemical Sciences (CES), Faculty of Chemistry and Biochemistry, Ruhr-Universität Bochum, Universitätsstr. 150, D-44780 Bochum, GermanyMore by Julian Szczesny
- João R. C. JunqueiraJoão R. C. JunqueiraAnalytical Chemistry─Center for Electrochemical Sciences (CES), Faculty of Chemistry and Biochemistry, Ruhr-Universität Bochum, Universitätsstr. 150, D-44780 Bochum, GermanyMore by João R. C. Junqueira
- Patricia Rodríguez-MaciáPatricia Rodríguez-MaciáDepartment of Inorganic Spectroscopy, Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34−36, D-45470 Mülheim an der Ruhr, GermanyMore by Patricia Rodríguez-Maciá
- James A. BirrellJames A. BirrellDepartment of Inorganic Spectroscopy, Max Planck Institute for Chemical Energy Conversion, Stiftstrasse 34−36, D-45470 Mülheim an der Ruhr, GermanyMore by James A. Birrell
- Felipe Conzuelo*Felipe Conzuelo*Email: [email protected]Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa, Av. da República, 2780-157 Oeiras, PortugalMore by Felipe Conzuelo
- Wolfgang Schuhmann*Wolfgang Schuhmann*Email: [email protected]Analytical Chemistry─Center for Electrochemical Sciences (CES), Faculty of Chemistry and Biochemistry, Ruhr-Universität Bochum, Universitätsstr. 150, D-44780 Bochum, GermanyMore by Wolfgang Schuhmann
Abstract
The development of electrodes for efficient CO2 reduction while forming valuable compounds is critical. The use of enzymes as catalysts provides the advantage of high catalytic activity in combination with highly selective transformations. We describe the electrical wiring of a carbon monoxide dehydrogenase II from Carboxydothermus hydrogenoformans (ChCODH II) using a cobaltocene-based low-potential redox polymer for the selective reduction of CO2 to CO over gas diffusion electrodes. High catalytic current densities of up to −5.5 mA cm–2 are achieved, exceeding the performance of previously reported bioelectrodes for CO2 reduction based on either carbon monoxide dehydrogenases or formate dehydrogenases. The proposed bioelectrode reveals considerable stability with a half-life of more than 20 h of continuous operation. Product quantification using gas chromatography confirmed the selective transformation of CO2 into CO without any parasitic co-reactions at the applied potentials.
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Introduction
Results and Discussion
Figure 1
Figure 1. Schematic representation of the redox polymer/enzyme gas diffusion electrode for CO2 reduction. The image includes an optical micrograph of the modified gas diffusion electrode, the electrografted layer of ethylenediamine, the structures of the redox polymer BPEI-[CoCp2], and the enzyme CODH II from C. hydrogenoformans (ChCODH II, PDB ID: 1SUF (30,31)).
Figure 2
Figure 2. Electrochemical characterization using (A) cyclic voltammetry and (B) amperometry of a BPEI-[CoCp2]/ChCODH II-modified gas diffusion electrode using Ar or CO2 applied to the backside of the electrode. Electrolyte: Ar-saturated 0.1 M phosphate buffer (pH 7.3). Scan rate in (A): 5 mV s–1. Applied potential in (B): −0.79 V vs SHE. Current densities were calculated with respect to the modified geometric surface area (d = 5 mm).
Figure 3
Figure 3. Faradaic efficiency calculated for the conversion of CO2 with a BPEI-[CoCp2]/ChCODH II-modified electrode. The bioelectrode was operated under constant turnover conditions (CO2, Eapp = −0.79 V vs SHE) in Ar-saturated 0.1 M phosphate buffer (pH 7.3). Error bars represent the standard deviation (n = 3).
Figure 4
Figure 4. Stability measurement under continuous turnover conditions with a BPEI-[CoCp2]/ChCODH II-modified gas diffusion electrode. Eapp = −0.79 V vs SHE. Electrolyte: Ar-saturated 0.1 M phosphate buffer (pH 7.3).
Conclusions
Experimental Section
Chemicals and Materials
Enzyme Expression and Purification
Redox Polymer Synthesis
Electrode Preparation
Electrochemical Measurements
Gas Chromatography
Supporting Information
The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acsami.2c09547.
Literature comparison; redox polymer characterization; gas chromatography setup and results; and voltammetric characterization before and after long-term measurement (PDF)
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Acknowledgments
The authors are grateful for financial support from the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) in the framework of the SPP2240 (e-biotech) [445820469] and the European Union’s Horizon 2020 research and innovation program under the Marie Skłodowska-Curie MSCA-ITN “ImplantSens” [813006]. J.A.B. acknowledges funding from the DFG SPP 1927 “Iron–Sulfur for Life” project (Project No. BI 2198/1-1) and the Max Planck Society. P.R.-M. thanks the University of Oxford for a Glasstone Research Fellowship and Linacre College Oxford for a Junior Research Fellowship.
References
This article references 31 other publications.
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- 4Ma, W.; He, X.; Wang, W.; Xie, S.; Zhang, Q.; Wang, Y. Electrocatalytic Reduction of CO2 and CO to Multi-Carbon Compounds over Cu-Based Catalysts. Chem. Soc. Rev. 2021, 50, 12897– 12914, DOI: 10.1039/D1CS00535AGoogle Scholar4https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXitFKqtLjK&md5=e6d0af591d622a59c47fffbfafb815cbElectrocatalytic reduction of CO2 and CO to multi-carbon compounds over Cu-based catalystsMa, Wenchao; He, Xiaoyang; Wang, Wei; Xie, Shunji; Zhang, Qinghong; Wang, YeChemical Society Reviews (2021), 50 (23), 12897-12914CODEN: CSRVBR; ISSN:0306-0012. (Royal Society of Chemistry)A review. The electrocatalytic redn. of CO2 with H2O to multi-carbon (C2+) compds., in particular, C2+ olefins and oxygenates, which have versatile applications in the chem. and energy industries, holds great potential to mitigate the depletion of fossil resources and abate carbon emissions. There are two major routes for the electrocatalytic CO2 redn. to C2+ compds., i.e., the direct route and the indirect route via CO. The electrocatalytic CO2 redn. to CO has been commercialised with solid oxide electrolyzers, making the indirect route via CO to C2+ compds. also a promising alternative. This tutorial review focuses on the similarities and differences in the electrocatalytic CO2 and CO redn. reactions (CO2RR and CORR) into C2+ compds., including C2H4, C2H5OH, CH3COO- and n-C3H7OH, over Cu-based catalysts. First, we introduce the fundamental aspects of the electrocatalytic reactions, including the cathode and anode reactions, electrocatalytic reactors and crucial performance parameters. Next, the reaction mechanisms, in particular, the C-C coupling mechanism, are discussed. Then, efficient catalysts and systems for these two reactions are critically reviewed. We analyze the key factors that det. the selectivity, activity and stability for the electrocatalytic CO2RR and CORR. Finally, the opportunities, challenges and future trends in the electrocatalytic CO2RR and CORR are proposed. These insights will offer guidance for the design of industrial-relevant catalysts and systems for the synthesis of C2+ olefins and oxygenates.
- 5Suominen, M.; Kallio, T. What we currently know about Carbon-Supported Metal and Metal Oxide Nanomaterials in Electrochemical CO2 Reduction. ChemElectroChem 2021, 8, 2397– 2406, DOI: 10.1002/celc.202100345Google Scholar5https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXhsVOmt7bN&md5=b4b203aad7f0ddd6d27942c0d3e13511What We Currently Know about Carbon-Supported Metal and Metal Oxide Nanomaterials in Electrochemical CO2 ReductionSuominen, Milla; Kallio, TanjaChemElectroChem (2021), 8 (13), 2397-2406CODEN: CHEMRA; ISSN:2196-0216. (Wiley-VCH Verlag GmbH & Co. KGaA)A review. Electrochem. redn. of CO2 is considered important in enhancing the circular-economy design; it can suppress harmful greenhouse-gas emissions while, combined with intermittent renewable energy sources, it can employ the surplus energy for prodn. of important chems. and fuels. In the process, electrocatalysts play an important role as the mediators of the highly active and selective conversion of CO2. Transition and post transition metals and their oxides are an important electrocatalyst group. For practical reasons, these metals need to be applied as nanoparticles supported on highly conducting materials enabling fabrication of 3D electrodes. In this mini, we focus on gathering our current knowledge on the effects which transition and post transition metal and metal oxide nanoparticles supported on different carbons may have on electrochem. redn. of CO2. We focus on literature of studies conducted in aq. conditions, under as similar conditions as possible, to ensure comparability. This approach enables us to highlight possible support effects and issues that complicate making conclusions on support effects.
- 6Wang, G.; Chen, J.; Ding, Y.; Cai, P.; Yi, L.; Li, Y.; Tu, C.; Hou, Y.; Wen, Z.; Dai, L. Electrocatalysis for CO2 Conversion: From Fundamentals to Value-Added Products. Chem. Soc. Rev. 2021, 50, 4993– 5061, DOI: 10.1039/D0CS00071JGoogle Scholar6https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXkvFKmt70%253D&md5=f43affba88dcc9183b0d298c53417079Electrocatalysis for CO2 conversion: from fundamentals to value-added productsWang, Genxiang; Chen, Junxiang; Ding, Yichun; Cai, Pingwei; Yi, Luocai; Li, Yan; Tu, Chaoyang; Hou, Yang; Wen, Zhenhai; Dai, LimingChemical Society Reviews (2021), 50 (8), 4993-5061CODEN: CSRVBR; ISSN:0306-0012. (Royal Society of Chemistry)A review. The continuously increasing CO2 released from human activities poses a great threat to human survival by fluctuating global climate and disturbing carbon balance among the four reservoirs of the biosphere, earth, air, and water. Converting CO2 to value-added feedstocks via electrocatalysis of the CO2 redn. reaction (CO2RR) has been regarded as one of the most attractive routes to re-balance the carbon cycle, thanks to its multiple advantages of mild operating conditions, easy handling, tunable products and the potential of synergy with the rapidly increasing renewable energy (i.e., solar, wind). Instead of focusing on a special topic of electrocatalysts for the CO2RR that have been extensively reviewed elsewhere, we herein present a rather comprehensive review of the recent research progress, in the view of assocd. value-added products upon selective electrocatalytic CO2 conversion. We initially provide an overview of the history and the fundamental science regarding the electrocatalytic CO2RR, with a special introduction to the design, prepn., and performance evaluation of electrocatalysts, the factors influencing the CO2RR, and the assocd. theor. calcns. Emphasis will then be given to the emerging trends of selective electrocatalytic conversion of CO2 into a variety of value-added products. The structure-performance relationship and mechanism will also be discussed and investigated. The outlooks for CO2 electrocatalysis, including the challenges and opportunities in the development of new electrocatalysts, electrolyzers, the recently rising operando fundamental studies, and the feasibility of industrial applications are finally summarized.
- 7Boutin, E.; Merakeb, L.; Ma, B.; Boudy, B.; Wang, M.; Bonin, J.; Anxolabéhère-Mallart, E.; Robert, M. Molecular Catalysis of CO2 reduction: Recent Advances and Perspectives in Electrochemical and Light-Driven Processes with Selected Fe, Ni and Co Aza Macrocyclic and Polypyridine Complexes. Chem. Soc. Rev. 2020, 49, 5772– 5809, DOI: 10.1039/D0CS00218FGoogle Scholar7https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXhsVags7rM&md5=13c4a6b0aabc350c8d040f22512aadc3Molecular catalysis of CO2 reduction: recent advances and perspectives in electrochemical and light-driven processes with selected Fe, Ni and Co aza macrocyclic and polypyridine complexesBoutin, E.; Merakeb, L.; Ma, B.; Boudy, B.; Wang, M.; Bonin, J.; Anxolabehere-Mallart, E.; Robert, M.Chemical Society Reviews (2020), 49 (16), 5772-5809CODEN: CSRVBR; ISSN:0306-0012. (Royal Society of Chemistry)A review. Earth-abundant Fe, Ni, and Co aza macrocyclic and polypyridine complexes have been thoroughly investigated for CO2 electrochem. and visible-light-driven redn. Since the first reports in the 1970s, an enormous body of work has been accumulated regarding the two-electron two-proton redn. of the gas, along with mechanistic and spectroscopic efforts to rationalize the reactivity and establish guidelines for structure-reactivity relationships. The ability to fine tune the ligand structure and the almost unlimited possibilities of designing new complexes have led to highly selective and efficient catalysts. Recent efforts toward developing hybrid systems upon combining mol. catalysts with conductive or semi-conductive materials have converged to high catalytic performances in water solns., to the inclusion of these catalysts into CO2 electrolyzers and photo-electrochem. devices, and to the discovery of catalytic pathways beyond two electrons. Combined with the continuous mechanistic efforts and new developments for in situ and in operando spectroscopic studies, mol. catalysis of CO2 redn. remains a highly creative approach.
- 8Azcarate, I.; Costentin, C.; Robert, M.; Savéant, J.-M. Through-Space Charge Interaction Substituent Effects in Molecular Catalysis Leading to the Design of the Most Efficient Catalyst of CO2-to-CO Electrochemical Conversion. J. Am. Chem. Soc. 2016, 138, 16639– 16644, DOI: 10.1021/jacs.6b07014Google Scholar8https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XhvVCjsLbP&md5=783b8c66f38a6449af876b6931182c85Through-Space Charge Interaction Substituent Effects in Molecular Catalysis Leading to the Design of the Most Efficient Catalyst of CO2-to-CO Electrochemical ConversionAzcarate, Iban; Costentin, Cyrille; Robert, Marc; Saveant, Jean-MichelJournal of the American Chemical Society (2016), 138 (51), 16639-16644CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)The starting point of this study of through space-substituent effects on the catalysis of the electrochem. CO2-to-CO conversion by iron(0)-tetra-Ph porphyrins is the linear free energy correlation between through-structure electronic effects and the iron(I/0) std. potential established in ref. 1. The introduction of four pos. charged trimethylanilinium groups in para-position of the TPP phenyls results in an important pos. deviation from the correlation and a parallel improvement of the catalytic Tafel plot. The assignment of this catalysis boosting effect to the coulombic interaction of these pos. charges with the neg. charge borne by the initial Fe0-CO2 adduct is confirmed by the neg. deviation obsd. when the four pos. charges are replaced by four neg. charges borne by sulfonate groups also installed in the para-position of the TPP phenyls. The climax of this strategy of catalysis boosting by coulombic stabilization of the initial Fe0-CO2 adduct is reached when four pos. charged trimethylanilinium groups are introduced in ortho-position of the TPP phenyls. The addn. of a large concn. of a weak acid - phenol helps cleaving one of the C-O bonds of CO2. The efficiency of the resulting catalyst is unprecedented as can be judged by catalytic Tafel plot benchmarking with all presently available catalysts of the electrochem. CO2-to-CO conversion. The maximal turnover frequency is ≤106 s-1 and is reached at an overpotential of only 220 mV; the turnover frequency at zero overpotential is larger than 300 s-1. This catalyst leads to a highly selective formation of CO (practically 100%) in spite of the presence of a high concn. of phenol which could have favor H2 evolution. It is also very stable showing no significant alteration after more than eighty hours electrolysis.
- 9Monti, D.; Ottolina, G.; Carrea, G.; Riva, S. Redox Reactions Catalyzed by Isolated Enzymes. Chem. Rev. 2011, 111, 4111– 4140, DOI: 10.1021/cr100334xGoogle Scholar9https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXltlaruro%253D&md5=e68132d4c7c6f44869a30763bbad722aRedox reactions catalyzed by isolated enzymesMonti, Daniela; Ottolina, Gianluca; Carrea, Giacomo; Riva, SergioChemical Reviews (Washington, DC, United States) (2011), 111 (7), 4111-4140CODEN: CHREAY; ISSN:0009-2665. (American Chemical Society)A review. The authors provide an overview of groups of oxidoreductases that are suitable for synthetic applications as isolated enzymes. The redox reactions catalyzed by these enzymes are numerous and varied. Included among the oxidoreductases discussed in detail are dehydrogenases, oxidases, oxygenases (including cytochromes P 450), and peroxidases.
- 10Meneghello, M.; Léger, C.; Fourmond, V. Electrochemical Studies of CO2-Reducing Metalloenzymes. Chem. – Eur. J. 2021, 27, 17542– 17553, DOI: 10.1002/chem.202102702Google Scholar10https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXitlams7zE&md5=819dcab4143e90872230ed6fd08b7d00Electrochemical Studies of CO2-Reducing MetalloenzymesMeneghello, Marta; Leger, Christophe; Fourmond, VincentChemistry - A European Journal (2021), 27 (70), 17542-17553CODEN: CEUJED; ISSN:0947-6539. (Wiley-VCH Verlag GmbH & Co. KGaA)A review. Only two enzymes are capable of directly reducing CO2: CO dehydrogenase, which produces CO at a [NiFe4S4] active site, and formate dehydrogenase, which produces formate at a mononuclear W or Mo active site. Both metalloenzymes are very rapid, energy-efficient and specific in terms of product. They have been connected to electrodes with two different objectives. A series of studies used protein film electrochem. to learn about different aspects of the mechanism of these enzymes (reactivity with substrates, inhibitors...). Another series focused on taking advantage of the catalytic performance of these enzymes to build biotechnol. devices, from CO2-reducing electrodes to full photochem. devices performing artificial photosynthesis. Here, we review all these works.
- 11Svetlitchnyi, V.; Peschel, C.; Acker, G.; Meyer, O. Two Membrane-Associated NiFeS-Carbon Monoxide Dehydrogenases from the Anaerobic Carbon-Monoxide-Utilizing Eubacterium Carboxydothermus Hydrogenoformans. J. Bacteriol. 2001, 183, 5134– 5144, DOI: 10.1128/JB.183.17.5134-5144.2001Google Scholar11https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3MXmtFKrs7k%253D&md5=361f94957baba8c8d84676c377519affTwo membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformansSvetlitchnyi, Vitali; Peschel, Christine; Acker, Georg; Meyer, OrtwinJournal of Bacteriology (2001), 183 (17), 5134-5144CODEN: JOBAAY; ISSN:0021-9193. (American Society for Microbiology)Two monofunctional NiFeS carbon monoxide (CO) dehydrogenases, designated CODH I and CODH II, were purified to homogeneity from the anaerobic CO-utilizing eubacterium Carboxydothermus hydrogenoformans. Both enzymes differ in their subunit mol. masses, N-terminal sequences, peptide maps, and immunol. reactivities. Immunogold labeling of ultrathin sections revealed both CODHs in assocn. with the inner aspect of the cytoplasmic membrane. Both enzymes catalyze the reaction CO + H2O → CO2 + 2 e- + 2 H+. Oxidized viologen dyes are effective electron acceptors. The specific enzyme activities were 15,756 (CODH I) and 13,828 (CODH II) μmol of CO oxidized min-1 mg-1 of protein (Me viologen, pH 8.0, 70°). The two enzymes oxidize CO very efficiently, as indicated by kcat/Km values at 70° of 1.3·109 M-1 CO s-1 (CODH I) and 1.7·109 M-1 CO s-1 (CODH II). The apparent Km values at pH 8.0 and 70° are 30 and 18 μM CO for CODH I and CODH II, resp. Acetyl CoA synthase activity is not assocd. with the enzymes. CODH I (125 kDa, 62.5-kDa subunit) and CODH II (129 kDa, 64.5-kDa subunit) are homodimers contg. 1.3 to 1.4 and 1.7 atoms of Ni, 20 to 22 and 20 to 24 atoms of Fe, and 22 and 19 atoms of acid-labile sulfur, resp. ESR (EPR) spectroscopy revealed signals indicative of [4Fe-4S] clusters. Ni was EPR silent under any conditions tested. It is proposed that CODH I is involved in energy generation and that CODH II serves in anabolic functions.
- 12Hille, R.; Dingwall, S.; Wilcoxen, J. The Aerobic CO Dehydrogenase from Oligotropha Carboxidovorans. J. Biol. Inorg. Chem. 2015, 20, 243– 251, DOI: 10.1007/s00775-014-1188-4Google Scholar12https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXhsVeku7rM&md5=bb16ded2286301af4b96e9653c8e49f2The aerobic CO dehydrogenase from Oligotropha carboxidovoransHille, Russ; Dingwall, Stephanie; Wilcoxen, JarettJBIC, Journal of Biological Inorganic Chemistry (2015), 20 (2), 243-251CODEN: JJBCFA; ISSN:0949-8257. (Springer)A review. The authors review the recent literature dealing with Mo- and Cu-dependent carbon monoxide dehydrogenase of O. carboxidovorans, with particular emphasis on the structure of the enzyme and recent advances in the understanding of the enzyme catalytic mechanism.
- 13Can, M.; Armstrong, F. A.; Ragsdale, S. W. Structure, Function, and Mechanism of the Nickel Metalloenzymes, CO Dehydrogenase, and Acetyl-CoA Synthase. Chem. Rev. 2014, 114, 4149– 4174, DOI: 10.1021/cr400461pGoogle Scholar13https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXisVWhtLo%253D&md5=e61881c21866dd429c6924d2d9f57335Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthaseCan, Mehmet; Armstrong, Fraser A.; Ragsdale, Stephen W.Chemical Reviews (Washington, DC, United States) (2014), 114 (8), 4149-4174CODEN: CHREAY; ISSN:0009-2665. (American Chemical Society)A review. There are 6 known pathways by which CO2 is fixed, with the Calvin cycle and photosynthesis providing most of the fixed carbon. Under anaerobic conditions, the Wood-Ljungdahl pathway is a predominant CO2 sink, and the Ni-contg. metalloenzymes, carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS), are the key enzymes in this pathway. Here, the structure, function, and catalytic mechanism of these 2 metalloenzymes, that have defined novel biochem. mechanisms involving organometallic chem. to catalyze their reactions, are discussed. CODH, esp. coupled to ACS and other enzymes of the Wood-Ljungdahl pathway, offers great potential for biotechnol. through the conversion of simple abundant compds. into needed chems. and fuels. Developing an industrial process that efficiently couples CO2 redn. to CO with a carbonylation reaction would be an important advance to the chem. industry because C-C bond formation by reactions with CO is instrumental in many industrial processes. CODH/ACS catalyze such a coupled process as an important component of the biol. carbon cycle. If fuels could be made from CO2, these C-C bond-forming reactions will be of even more importance in energy generation.
- 14Lindahl, P. A. The Ni-Containing Carbon Monoxide Dehydrogenase Family: Light at the End of the Tunnel?. Biochemistry 2002, 41, 2097– 2105, DOI: 10.1021/bi015932+Google Scholar14https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD38Xns1KhsA%253D%253D&md5=e8037b60c521ec0f02df429cc7a080dbThe Ni-Containing Carbon Monoxide Dehydrogenase Family: Light at the End of the Tunnel?Lindahl, Paul A.Biochemistry (2002), 41 (7), 2097-2105CODEN: BICHAW; ISSN:0006-2960. (American Chemical Society)A review on characterization, x-ray structure, and spectroscopic and redox properties of the Ni-contg. CO dehydrogenase (CODH) family of enzymes. The complexity and functional unity of the metal center structures, tunnels, and catalytic mechanisms employed by the CODH family of enzymes are discussed.
- 15Jeoung, J.-H.; Dobbek, H. Carbon Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide Dehydrogenase. Science 2007, 318, 1461– 1464, DOI: 10.1126/science.1148481Google Scholar15https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD2sXhtlGmtLbO&md5=ced0378cfcee05f1b3aae1553acae5acCarbon Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide DehydrogenaseJeoung, Jae-Hun; Dobbek, HolgerScience (Washington, DC, United States) (2007), 318 (5855), 1461-1464CODEN: SCIEAS; ISSN:0036-8075. (American Association for the Advancement of Science)Anaerobic CO dehydrogenases catalyze the reversible oxidn. of CO to CO2 at a complex Ni-, Fe-, and S-contg. metal center called cluster C. We report crystal structures of CO dehydrogenase II from Carboxydothermus hydrogenoformans in three different states. In a reduced state, exogenous CO2 supplied in soln. is bound and reductively activated by cluster C. In the intermediate structure, CO2 acts as a bridging ligand between Ni and the asym. coordinated Fe, where it completes the square-planar coordination of the Ni ion. It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidn. and CO2 redn. at the Ni-Fe site of cluster C.
- 16Contaldo, U.; Guigliarelli, B.; Perard, J.; Rinaldi, C.; Le Goff, A.; Cavazza, C. Efficient Electrochemical CO2/CO Interconversion by an Engineered Carbon Monoxide Dehydro-genase on a Gas-Diffusion Carbon Nanotube-Based Bioelectrode. ACS Catal. 2021, 11, 5808– 5817, DOI: 10.1021/acscatal.0c05437Google Scholar16https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXpsFGgsLk%253D&md5=057d0326e7144e3a2fbbd36aa063db03Efficient Electrochemical CO2/CO Interconversion by an Engineered Carbon Monoxide Dehydrogenase on a Gas-Diffusion Carbon Nanotube-Based BioelectrodeContaldo, Umberto; Guigliarelli, Bruno; Perard, Julien; Rinaldi, Clara; Le Goff, Alan; Cavazza, ChristineACS Catalysis (2021), 11 (9), 5808-5817CODEN: ACCACS; ISSN:2155-5435. (American Chemical Society)Carbon monoxide dehydrogenase catalyzes the reversible oxidn. of CO to CO2. The monofunctional enzyme from Rhodospirillum rubrum (RrCODH) has been extensively characterized in the past, although its use and investigation by bioelectrochem. have been limited. Here, we developed a heterologous system yielding a highly stable and active recombinant RrCODH in one-step purifn., with CO oxidn. activity reaching a max. of 26 500 U·mg-1, making RrCODH the most active CODH under ambient conditions described so far. ESR was used to precisely characterize the recombinant RrCODH, demonstrating the integrity of the active site. Selective CO2/CO interconversion with max. turnover frequencies of 150 s-1 for CO oxidn. (1.5 mA cm-2 at 250 mV overpotential) and 420 s-1 for CO2 redn. (4.2 mA cm-2 at 180 mV overpotential) is catalyzed by the recombinant RrCODH immobilized on MWCNT electrodes modified with 1-pyrenebutyric acid adamantyl amide (MWCNTADA), either in a classic three-electrode cell or in specifically designed CO2/CO-diffusing electrodes. This functional device is stable for hours with a turnover no. of at least 800 000. The performances of recombinant RrCODH-modified MWCNTADA are close to the best metal-based and mol.-based catalysts. These results greatly increase the benchmark for bioelectrocatalysis of reversible CO2 conversion.
- 17Dobbek, H.; Svetlitchnyi, V.; Gremer, L.; Huber, R.; Meyer, O. Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a Ni-4Fe-5S Cluster. Science 2001, 293, 1281– 1285, DOI: 10.1126/science.1061500Google Scholar17https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3MXmtFCrtr4%253D&md5=72c4c709d2985f28dc7732c0b4c804e7Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] clusterDobbek, Holger; Svetlitchnyi, Vitali; Gremer, Lothar; Huber, Robert; Meyer, OrtwinScience (Washington, DC, United States) (2001), 293 (5533), 1281-1285CODEN: SCIEAS; ISSN:0036-8075. (American Association for the Advancement of Science)The homodimeric Ni-contg. carbon monoxide dehydrogenase (I) from the anaerobic bacterium, Carboxydothermus hydrogenoformans, catalyzes the oxidn. of CO to CO2. Here, the crystal structure of reduced I was solved at 1.6 Å resoln. This structure represents the prototype for Ni-contg. I from anaerobic bacteria and archae. I contained 5 metal clusters, of which clusters B, B', and a subunit-bridging, surface-exposed cluster D, were cubane-type [4Fe-4S] clusters. I active site clusters C and C' were novel, asym. [Ni-4Fe-5S] clusters. The integral Ni ion, which is the likely site of CO oxidn., was coordinated by 4 S ligands with square planar geometry.
- 18Contaldo, U.; Curtil, M.; Pérard, J.; Cavazza, C.; Le Goff, A. A Pyrene-Triazacyclononane Anchor Affords High Operational Stability for CO2 RR by a CNT-Supported Histidine-Tagged CODH. Angew. Chem., Int. Ed. 2022, e202117212 DOI: 10.1002/anie.202117212Google Scholar18https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38XnvFajt78%253D&md5=ca6917011789f536edc1876d4f3ba256A Pyrene-Triazacyclononane Anchor Affords High Operational Stability for CO2RR by a CNT-Supported Histidine-Tagged CODHContaldo, Umberto; Curtil, Mathieu; Perard, Julien; Cavazza, Christine; Le Goff, AlanAngewandte Chemie, International Edition (2022), 61 (21), e202117212CODEN: ACIEF5; ISSN:1433-7851. (Wiley-VCH Verlag GmbH & Co. KGaA)An original 1-acetato-4-(1-pyrenyl)-1,4,7-triazacyclononane (AcPyTACN) was synthesized for the immobilization of a His-tagged recombinant CODH from Rhodospirillum rubrum (RrCODH) on carbon-nanotube electrodes. The strong binding of the enzyme at the Ni-AcPyTACN complex affords a high c.d. of 4.9 mA cm-2 towards electroenzymic CO2 redn. and a high stability of more than 6x106 TON when integrated on a gas-diffusion bioelectrode.
- 19Habermüller, K.; Mosbach, M.; Schuhmann, W. Electron-Transfer Mechanisms in Amperometric Biosensors. Fresenius’ J. Anal. Chem. 2000, 366, 560– 568, DOI: 10.1007/s002160051551Google Scholar19https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3cXhvF2lsr8%253D&md5=693c360d6d9f783fe808be972a53b5dfElectron-transfer mechanisms in amperometric biosensorsHabermuller, K.; Mosbach, M.; Schuhmann, W.Fresenius' Journal of Analytical Chemistry (2000), 366 (6-7), 560-568CODEN: FJACES; ISSN:0937-0633. (Springer-Verlag)Review with 156 refs. The function of amperometric biosensors is related to electron-transfer processes between the active site of an (immobilized) enzyme and an electrode surface which is poised to an appropriate working potential. Problems and specific features of architectures for amperometric biosensors using different electron-transfer pathways such as mediated electron transfer, electron-hopping in redox polymers, electron transfer using mediator-modified enzymes and carbon-paste electrodes, direct electron transfer by means of self-assembled monolayers or via conducting-polymer chains are discussed.
- 20Shin, W.; Lee, S. H.; Shin, J. W.; Lee, S. P.; Kim, Y. Highly Selective Electrocatalytic Conversion of CO2 to CO at −0.57 V (NHE) by Carbon Monoxide Dehydrogenase from Moorella Thermoacetica. J. Am. Chem. Soc. 2003, 125, 14688– 14689, DOI: 10.1021/ja037370iGoogle Scholar20https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3sXovVCltrc%253D&md5=a924cfe05aaff5bc843f56a566a8f3faHighly Selective Electrocatalytic Conversion of CO2 to CO at -0.57 V (NHE) by Carbon Monoxide Dehydrogenase from Moorella thermoaceticaShin, Woonsup; Lee, Sang Hee; Shin, Jun Won; Lee, Sang Phil; Kim, YousungJournal of the American Chemical Society (2003), 125 (48), 14688-14689CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)We found that CODH is a fascinating enzyme for the electrochem. conversion of CO2 to CO. It could reduce CO2 to CO at -0.57 V vs. NHE with ∼100% current efficiency in 0.1 M phosphate buffer (pH 6.3). Nature's unique structure of C-cluster in CODH would be responsible for the low overpotential and the selective and fast conversion of CO2. The turnover no. per C-cluster is 700 h-1, and the pH optimum is 6.3.
- 21Schuhmann, W.; Wohlschläger, H.; Lammert, R.; Schmidt, H.-L.; Löffler, U.; Wiemhöfer, H.-D.; Göpel, W. Leaching of Dimethylferrocene, a Redox Mediator in Amperometric Enzyme Electrodes. Sens. Actuators, B 1990, 1, 571– 575, DOI: 10.1016/0925-4005(90)80275-5Google ScholarThere is no corresponding record for this reference.
- 22Heller, A. Electron-Conducting Redox Hydrogels: Design, Characteristics and Synthesis. Curr. Opin. Chem. Biol. 2006, 10, 664– 672, DOI: 10.1016/j.cbpa.2006.09.018Google Scholar22https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD28Xht1Kgu7nN&md5=c643c609596159d0c91a5da79f7f5962Electron-conducting redox hydrogels: design, characteristics and synthesisHeller, AdamCurrent Opinion in Chemical Biology (2006), 10 (6), 664-672CODEN: COCBF4; ISSN:1367-5931. (Elsevier B.V.)A review. Redox hydrogels constitute the only electron-conducting phase in which water-sol. chems. and biochems. dissolve and diffuse. The combination of soly. and diffusion makes the electron-conducting gels permeable to water-sol. biochems. and chems. The electron-conducting redox hydrogels serve to elec. connect the redox centers of enzymes to electrodes, enabling their use whenever leaching of electron-shuttling diffusional redox mediators must be avoided, which is the case in s.c. implanted biosensors for diabetes management and in miniature, potentially implantable, glucose-O2 biofuel cells. Because the hydrogels envelope the redox enzymes, they elec. wire the reaction centers to electrodes irresp. of spatial orientation and connect to electrode redox centers of multiple enzyme layers. Hence, the attained current densities of enzyme substrate electrooxidn. or electroredn. are much higher than with enzyme monolayers packed onto electrode surfaces.
- 23Tapia, C.; Milton, R. D.; Pankratova, G.; Minteer, S. D.; Åkerlund, H.-E.; Leech, D.; De Lacey, A. L.; Pita, M.; Gorton, L. Wiring of Photosystem I and Hydrogenase on an Electrode for Photoelectrochemical H2 Production by Using Redox Polymers for Relatively Positive Onset Potential. ChemElectroChem 2017, 4, 90– 95, DOI: 10.1002/celc.201600506Google Scholar23https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XhsFymsLzO&md5=23e9cfdf9901b68a7c4962fdba0d00dbWiring of Photosystem I and Hydrogenase on an Electrode for Photoelectrochemical H2 Production by using Redox Polymers for Relatively Positive Onset PotentialTapia, Cristina; Milton, Ross D.; Pankratova, Galina; Minteer, Shelley D.; Aakerlund, Hans-Erik; Leech, Donal; De Lacey, Antonio L.; Pita, Marcos; Gorton, LoChemElectroChem (2017), 4 (1), 90-95CODEN: CHEMRA; ISSN:2196-0216. (Wiley-VCH Verlag GmbH & Co. KGaA)Photosystem I (PSI) is combined with Desulfovibrio gigas hydrogenase for the bioelectrocatalytic photosynthesis of hydrogen at an electrode surface. The activity of these two biocatalysts is linked by two redox polymers; a redox polymer with a relatively pos. potential (loaded with an Os complex) is able to reduce PSI and thus facilitates the prodn. of photoexcited electrons, whereas redox polymers of relatively low potential are able to transfer electrons to the hydrogenase. Two neg.-potential redox polymers are tested, with either a viologen pendant (4-methyl-4'-bromopropylviologen functionalized linear polyethylenimine) or a cobaltocene pendant (cobaltocene-functionalized branched polyethylenimine, Cc-BPEI). Both are able to protect hydrogenase from O2 inactivation, but only the use of Cc-BPEI yields significant photocurrents for H+ redn., likely due to its lower redox potential. The photocurrents obtained are found to be proportional to the quantity of H2 produced, reaching a max. of -30 μA cm-2 for the system incorporating Cc-BPEI and showing a relatively pos. onset potential at +0.38 V vs. SHE.
- 24Yuan, M.; Sahin, S.; Cai, R.; Abdellaoui, S.; Hickey, D. P.; Minteer, S. D.; Milton, R. D. Creating a Low-Potential Redox Polymer for Efficient Electroenzymatic CO2 Reduction. Angew. Chem., Int. Ed. 2018, 57, 6582– 6586, DOI: 10.1002/anie.201803397Google Scholar24https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXosFyis7c%253D&md5=3738a50cd73cc5a56551bf5304b34046Creating a Low-Potential Redox Polymer for Efficient Electroenzymatic CO2 ReductionYuan, Mengwei; Sahin, Selmihan; Cai, Rong; Abdellaoui, Sofiene; Hickey, David P.; Minteer, Shelley D.; Milton, Ross D.Angewandte Chemie, International Edition (2018), 57 (22), 6582-6586CODEN: ACIEF5; ISSN:1433-7851. (Wiley-VCH Verlag GmbH & Co. KGaA)Increasing greenhouse gas emissions have resulted in greater motivation to find novel carbon dioxide (CO2) redn. technologies, where the redn. of CO2 to valuable chem. commodities is desirable. Molybdenum-dependent formate dehydrogenase (Mo-FDH) from Escherichia coli is a metalloenzyme that is able to interconvert formate and CO2. We describe a low-potential redox polymer, synthesized by a facile method, that contains cobaltocene (grafted to poly(allylamine), Cc-PAA) to simultaneously mediate electrons to Mo-FDH and immobilize Mo-FDH at the surface of a carbon electrode. The resulting bioelectrode reduces CO2 to formate with a high Faradaic efficiency of 99±5 % at a mild applied potential of -0.66 V vs. SHE.
- 25So, K.; Sakai, K.; Kano, K. Gas Diffusion Bioelectrodes. Curr. Opin. Electrochem. 2017, 5, 173– 182, DOI: 10.1016/j.coelec.2017.09.001Google Scholar25https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXhtVGgsLfL&md5=e57c38d24b4c8a3d20a414c0ef53fc9bGas diffusion bioelectrodesSo, Keisei; Sakai, Kento; Kano, KenjiCurrent Opinion in Electrochemistry (2017), 5 (1), 173-182CODEN: COEUCY; ISSN:2451-9111. (Elsevier B.V.)A review. Currently, bioelectrocatalytic devices such as biofuel cells and bioreactors are recognized as new environment-friendly devices for the prodn. of electricity and valuable products. Thus far, systems have been improved from the viewpoints of enzymes and electrodes. A gas diffusion bioelectrode (GDBE) is one of the best approaches to improve electrode systems. This system has been remarkably developed and essentially employed in bioelectrocatalytic systems with gaseous substrates to realize high-speed H2 oxidn. and O2 redn. for biofuel cells and to realize the high-speed bioelectrocatalytic redn. of CO2. GDBEs permit the enzymes to directly use gaseous substrates, and it is imperative that the electrodes exhibit suitable porosity, cond., and hydrophobicity/hydrophilicity balance for the gas permeation and enzyme reaction at the bio-three-phase interface of GDBEs. In this review article, the major factors of GDBEs are discussed by highlighting recent remarkable contributions and challenges.
- 26Szczesny, J.; Birrell, J. A.; Conzuelo, F.; Lubitz, W.; Ruff, A.; Schuhmann, W. Redox-Polymer-Based High-Current-Density Gas-Diffusion H2-Oxidation Bioanode Using FeFe Hydrogenase from Desulfovibrio Desulfuricans in a Membrane-Free Biofuel Cell. Angew. Chem., Int. Ed. 2020, 59, 16506– 16510, DOI: 10.1002/anie.202006824Google Scholar26https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXhsVakur7J&md5=542ae01bb1ee951c068a19ef2a4a4143Redox-Polymer-Based High-Current-Density Gas-Diffusion H2-Oxidation Bioanode Using [FeFe] Hydrogenase from Desulfovibrio desulfuricans in a Membrane-free Biofuel CellSzczesny, Julian; Birrell, James A.; Conzuelo, Felipe; Lubitz, Wolfgang; Ruff, Adrian; Schuhmann, WolfgangAngewandte Chemie, International Edition (2020), 59 (38), 16506-16510CODEN: ACIEF5; ISSN:1433-7851. (Wiley-VCH Verlag GmbH & Co. KGaA)The incorporation of highly active but also highly sensitive catalysts (e.g. the [FeFe] hydrogenase from Desulfovibrio desulfuricans) in biofuel cells is still one of the major challenges in sustainable energy conversion. We report the fabrication of a dual-gas diffusion electrode H2/O2 biofuel cell equipped with a [FeFe] hydrogenase/redox polymer-based high-current-d. H2-oxidn. bioanode. The bioanodes show benchmark current densities of around 14 mA cm-2 and the corresponding fuel cell tests exhibit a benchmark for a hydrogenase/redox polymer-based biofuel cell with outstanding power densities of 5.4 mW cm-2 at 0.7 V cell voltage. Furthermore, the highly sensitive [FeFe] hydrogenase is protected against oxygen damage by the redox polymer and can function under 5 % O2.
- 27Lielpetere, A.; Becker, J. M.; Szczesny, J.; Conzuelo, F.; Ruff, A.; Birrell, J.; Lubitz, W.; Schuhmann, W. Enhancing the Catalytic Current Response of H2 Oxidation Gas Diffusion Bioelectrodes Using an Optimized Viologen-Based Redox Polymer and [NiFe] Hydrogenase. ELSA 2022, 2, e2100100 DOI: 10.1002/elsa.202100100Google ScholarThere is no corresponding record for this reference.
- 28Ruff, A.; Szczesny, J.; Vega, M.; Zacarias, S.; Matias, P. M.; Gounel, S.; Mano, N.; Pereira, I. A. C.; Schuhmann, W. Redox-Polymer-Wired NiFeSe Hydrogenase Variants with Enhanced O2 Stability for Triple-Protected High-Current-Density H2-Oxidation Bioanodes. ChemSusChem 2020, 13, 3627– 3635, DOI: 10.1002/cssc.202000999Google Scholar28https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXhtFWlsLjN&md5=59543c3bae56f90b36d93dd98fd12b3fRedox-Polymer-Wired [NiFeSe] Hydrogenase Variants with Enhanced O2 Stability for Triple-Protected High-Current-Density H2-Oxidation BioanodesRuff, Adrian; Szczesny, Julian; Vega, Maria; Zacarias, Sonia; Matias, Pedro M.; Gounel, Sebastien; Mano, Nicolas; Pereira, Ines A. C.; Schuhmann, WolfgangChemSusChem (2020), 13 (14), 3627-3635CODEN: CHEMIZ; ISSN:1864-5631. (Wiley-VCH Verlag GmbH & Co. KGaA)Variants of the highly active [NiFeSe] hydrogenase from D. vulgaris Hildenborough that exhibit enhanced O2 tolerance were used as H2-oxidn. catalysts in H2/O2 biofuel cells. Two [NiFeSe] variants were elec. wired by means of low-potential viologen-modified redox polymers and evaluated with respect to H2-oxidn. and stability against O2 in the immobilized state. The two variants showed max. current densities of (450±84) μA cm-2 for G491A and (476±172) μA cm-2 for variant G941S on glassy carbon electrodes and a higher O2 tolerance than the wild type. In addn., the polymer protected the enzyme from O2 damage and high-potential inactivation, establishing a triple protection for the bioanode. The use of gas-diffusion bioanodes provided current densities for H2-oxidn. of up to 6.3 mA cm-2. Combination of the gas-diffusion bioanode with a bilirubin oxidase-based gas-diffusion O2-reducing biocathode in a membrane-free biofuel cell under anode-limiting conditions showed unprecedented benchmark power densities of 4.4 mW cm-2 at 0.7 V and an open-circuit voltage of 1.14 V even at moderate catalyst loadings, outperforming the previously reported system obtained with the [NiFeSe] wild type and the [NiFe] hydrogenase from D. vulgaris Miyazaki F.
- 29Szczesny, J.; Ruff, A.; Oliveira, A. R.; Pita, M.; Pereira, I. A. C.; de Lacey, A. L.; Schuhmann, W. Electroenzymatic CO2 Fixation Using Redox Polymer/Enzyme-Modified Gas Diffusion Electrodes. ACS Energy Lett. 2020, 5, 321– 327, DOI: 10.1021/acsenergylett.9b02436Google Scholar29https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXisVygt7vJ&md5=7aa761f577b595e421e3d689b9a0e574Electroenzymatic CO2 Fixation Using Redox Polymer/Enzyme-Modified Gas Diffusion ElectrodesSzczesny, Julian; Ruff, Adrian; Oliveira, Ana R.; Pita, Marcos; Pereira, Ines A. C.; De Lacey, Antonio L.; Schuhmann, WolfgangACS Energy Letters (2020), 5 (1), 321-327CODEN: AELCCP; ISSN:2380-8195. (American Chemical Society)The authors describe the fabrication of gas diffusion electrodes modified with polymer/enzyme layers for electroenzymic CO2 fixation. For this, a metal-free org. low-potential viologen-modified polymer was synthesized that reveals a redox potential of ∼-0.39 V vs. SHE and is thus able to elec. wire W-dependent formate dehydrogenase from Desulfovibrio vulgaris Hildenborough, which reversibly catalyzes the conversion of CO2 to formate. The use of gas diffusion electrodes eliminates limitations arising from slow mass transport when solid carbonate was used as CO2 source. The electrodes showed satisfactory stability that allowed for their long-term electrolysis application for electroenzymic formate prodn.
- 30Sehnal, D.; Bittrich, S.; Deshpande, M.; Svobodová, R.; Berka, K.; Bazgier, V.; Velankar, S.; Burley, S. K.; Koča, J.; Rose, A. S. Mol* Viewer: Modern Web App for 3D Visualization and Analysis of Large Biomolecular Structures. Nucleic Acids Res. 2021, 49, W431– W437, DOI: 10.1093/nar/gkab314Google Scholar30https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXhvV2isLbE&md5=ca2af5f4d0fa7758fcb0aaaf758790deMol* viewer: modern web app for 3D visualization and analysis of large biomolecular structuresSehnal, David; Bittrich, Sebastian; Deshpande, Mandar; Svobodova, Radka; Berka, Karel; Bazgier, Vaclav; Velankar, Sameer; Burley, Stephen K.; Koca, Jaroslav; Rose, Alexander S.Nucleic Acids Research (2021), 49 (W1), W431-W437CODEN: NARHAD; ISSN:1362-4962. (Oxford University Press)Large biomol. structures are being detd. exptl. on a daily basis using established techniques such as crystallog. and electron microscopy. In addn., emerging integrative or hybrid methods (I/HM) are producing structural models of huge macromol. machines and assemblies, sometimes contg. 100s of millions of non-hydrogen atoms. The performance requirements for visualization and anal. tools delivering these data are increasing rapidly. Significant progress in developing online, web-native three-dimensional (3D) visualization tools was previously accomplished with the introduction of the LiteMol suite and NGL Viewers. Thereafter, Mol* development was jointly initiated by PDBe and RCSB PDB to combine and build on the strengths of LiteMol (developed by PDBe) and NGL (developed by RCSB PDB). The web-native Mol* Viewer enables 3D visualization and streaming of macromol. coordinate and exptl. data, together with capabilities for displaying structure quality, functional, or biol. context annotations. High-performance graphics and data management allows users to simultaneously visualise up to hundreds of (superimposed) protein structures, stream mol. dynamics simulation trajectories, render cell-level models, or display huge I/HM structures. It is the primary 3D structure viewer used by PDBe and RCSB PDB. It can be easily integrated into third-party services.
- 31Dobbek, H.; Svetlitchnyi, V.; Liss, J.; Meyer, O. Carbon Monoxide Induced Decomposition of the Active Site Ni-4Fe-5S Cluster of CO Dehydrogenase. J. Am. Chem. Soc. 2004, 126, 5382– 5387, DOI: 10.1021/ja037776vGoogle Scholar31https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD2cXis1Cju7o%253D&md5=d9f6ccfac15712f1106df252645d60d0Carbon Monoxide Induced Decomposition of the Active Site [Ni-4Fe-5S] Cluster of CO DehydrogenaseDobbek, Holger; Svetlitchnyi, Vitali; Liss, Jago; Meyer, OrtwinJournal of the American Chemical Society (2004), 126 (17), 5382-5387CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)During the past two years, crystal structures of Cu- and Mo-contg. carbon monoxide dehydrogenases (CODHs) and Ni- and Fe-contg. CODHs have been reported. The active site of CODHs from anaerobic bacteria (cluster C) is composed of Ni, Fe, and S for which crystallog. studies of the enzymes from Carboxydothermus hydrogenoformans, Rhodospirillum rubrum, and Moorella thermoacetica revealed structural similarities in the overall protein fold but showed substantial differences in the essential Ni coordination environment. The [Ni-4Fe-5S] cluster C in the fully catalytically competent dithionite-reduced CODH II from C. hydrogenoformans (CODHIICh) at 1.6 Å resoln. contains a characteristic μ2-sulfido ligand between Ni and Fe1, resulting in a square-planar ligand arrangement with four S-ligands at the Ni ion. In contrast, the [Ni-4Fe-4S] clusters C in CO-treated CODH from R. rubrum resolved at 2.8 Å and in CO-treated acetyl-CoA synthase/CODH complex from M. thermoacetica at 2.2 and 1.9 Å resoln., resp., do not contain the μ2-sulfido ligand between Ni and Fe1 and display dissimilar geometries at the Ni ion. The [Ni-4Fe-4S] cluster is composed of a cubane [Ni-3Fe-4S] cluster linked to a mononuclear Fe site. The described coordination geometries of the Ni ion in the [Ni-4Fe-4S] cluster of R. rubrum and M. thermoacetica deviate from the square-planar ligand geometry in the [Ni-4Fe-5S] cluster C of CODHIICh. In addn., the latter was converted into a [Ni-4Fe-4S] cluster under specific conditions. The objective of this study was to elucidate the relationship between the structure of cluster C in CODHIICh and the functionality of the protein. The authors have detd. the CO oxidn. activity of CODHIICh under different conditions of crystn., prepd. crystals of the enzyme in the presence of dithiothreitol or dithionite as reducing agents under an atm. of N2 or CO, and solved the corresponding structures at 1.1 to 1.6 Å resolns. Fully active CODHIICh obtained after incubation of the enzyme with dithionite under N2 revealed the [Ni-4Fe-5S] cluster. Short treatment of the enzyme with CO in the presence of dithiothreitol resulted in a catalytically competent CODHIICh with a CO-reduced [Ni-4Fe-5S] cluster, but a prolonged treatment with CO caused the loss of CO-oxidizing activity and revealed a [Ni-4Fe-4S] cluster, which did not contain a μ2-S. These data suggest that the [Ni-4Fe-4S] cluster of CODHIICh is an inactivated decompn. product originating from the [Ni-4Fe-5S] cluster.
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Abstract
Figure 1
Figure 1. Schematic representation of the redox polymer/enzyme gas diffusion electrode for CO2 reduction. The image includes an optical micrograph of the modified gas diffusion electrode, the electrografted layer of ethylenediamine, the structures of the redox polymer BPEI-[CoCp2], and the enzyme CODH II from C. hydrogenoformans (ChCODH II, PDB ID: 1SUF (30,31)).
Figure 2
Figure 2. Electrochemical characterization using (A) cyclic voltammetry and (B) amperometry of a BPEI-[CoCp2]/ChCODH II-modified gas diffusion electrode using Ar or CO2 applied to the backside of the electrode. Electrolyte: Ar-saturated 0.1 M phosphate buffer (pH 7.3). Scan rate in (A): 5 mV s–1. Applied potential in (B): −0.79 V vs SHE. Current densities were calculated with respect to the modified geometric surface area (d = 5 mm).
Figure 3
Figure 3. Faradaic efficiency calculated for the conversion of CO2 with a BPEI-[CoCp2]/ChCODH II-modified electrode. The bioelectrode was operated under constant turnover conditions (CO2, Eapp = −0.79 V vs SHE) in Ar-saturated 0.1 M phosphate buffer (pH 7.3). Error bars represent the standard deviation (n = 3).
Figure 4
Figure 4. Stability measurement under continuous turnover conditions with a BPEI-[CoCp2]/ChCODH II-modified gas diffusion electrode. Eapp = −0.79 V vs SHE. Electrolyte: Ar-saturated 0.1 M phosphate buffer (pH 7.3).
References
This article references 31 other publications.
- 1Solomon, S.; Plattner, G.-K.; Knutti, R.; Friedlingstein, P. Irreversible Climate Change due to Carbon Dioxide Emissions. Proc. Natl. Acad. Sci. U. S. A. 2009, 106, 1704– 1709, DOI: 10.1073/pnas.08127211061https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD1MXitV2jur8%253D&md5=ccae2a0590b660dff586746e7bd8ec1cIrreversible climate change due to carbon dioxide emissionsSolomon, Susan; Plattner, Gian-Kasper; Knutti, Reto; Friedlingstein, PierreProceedings of the National Academy of Sciences of the United States of America (2009), 106 (6), 1704-1709CODEN: PNASA6; ISSN:0027-8424. (National Academy of Sciences)The severity of damaging human-induced climate change depends not only on the magnitude of the change but also on the potential for irreversibility. This paper shows that the climate change that takes place due to increases in carbon dioxide concn. is largely irreversible for 1000 years after emissions stop. Following cessation of emissions, removal of atm. carbon dioxide decreases radiative forcing, but is largely compensated by slower loss of heat to the ocean, so that atm. temps. do not drop significantly for at least 1,000 years. Among illustrative irreversible impacts that should be expected if atm. carbon dioxide concns. increase from current levels near 385 ppm by vol. (ppmv) to a peak of 450-600 ppmv over the coming century are irreversible dry-season rainfall redns. in several regions comparable to those of the "dust bowl" era and inexorable sea level rise. Thermal expansion of the warming ocean provides a conservative lower limit to irreversible global av. sea level rise of at least 0.4-1.0 m if 21st century CO2 concns. exceed 600 ppmv and 0.6-1.9 m for peak CO2 concns. exceeding ≈1,000 ppmv. Addnl. contributions from glaciers and ice sheet contributions to future sea level rise are uncertain but may equal or exceed several meters over the next millennium or longer.
- 2Finn, C.; Schnittger, S.; Yellowlees, L. J.; Love, J. B. Molecular Approaches to the Electrochemical Reduction of Carbon Dioxide. Chem. Commun. 2012, 48, 1392– 1399, DOI: 10.1039/C1CC15393E2https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC38XmtF2mtA%253D%253D&md5=874338f5fbf4a59297315b1c6e1200dbMolecular approaches to the electrochemical reduction of carbon dioxideFinn, Colin; Schnittger, Sorcha; Yellowlees, Lesley J.; Love, Jason B.Chemical Communications (Cambridge, United Kingdom) (2012), 48 (10), 1392-1399CODEN: CHCOFS; ISSN:1359-7345. (Royal Society of Chemistry)A review is given on recent progress in the exploitation of CO2 as a chem. feedstock. In particular, the design and development of mol. complexes that can act as catalysts for the electrochem. redn. of CO2 is highlighted, and compared to other biol., metal- and nonmetal-based systems.
- 3Jin, S.; Hao, Z.; Zhang, K.; Yan, Z.; Chen, J. Advances and Challenges for the Electrochemical Reduction of CO2 to CO: From Fundamentals to Industrialization. Angew. Chem., Int. Ed. 2021, 60, 20627– 20648, DOI: 10.1002/anie.2021018183https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXhtVCktrrF&md5=955638049b7104c9ad9dc2a91eb62178Advances and Challenges for the Electrochemical Reduction of CO2 to CO: From Fundamentals to IndustrializationJin, Song; Hao, Zhimeng; Zhang, Kai; Yan, Zhenhua; Chen, JunAngewandte Chemie, International Edition (2021), 60 (38), 20627-20648CODEN: ACIEF5; ISSN:1433-7851. (Wiley-VCH Verlag GmbH & Co. KGaA)A review. The electrochem. carbon dioxide redn. reaction (CO2RR) provides an attractive approach to convert renewable electricity into fuels and feedstocks in the form of chem. bonds. Among the different CO2RR pathways, the conversion of CO2 into CO is considered one of the most promising candidate reactions because of its high technol. and economic feasibility. Integrating catalyst and electrolyte design with an understanding of the catalytic mechanism will yield scientific insights and promote this technol. towards industrial implementation. Herein, we give an overview of recent advances and challenges for the selective conversion of CO2 into CO. Multidimensional catalyst and electrolyte engineering for the CO2RR are also summarized. Furthermore, recent studies on the large-scale prodn. of CO are highlighted to facilitate industrialization of the electrochem. redn. of CO2. To conclude, the remaining technol. challenges and future directions for the industrial application of the CO2RR to generate CO are highlighted.
- 4Ma, W.; He, X.; Wang, W.; Xie, S.; Zhang, Q.; Wang, Y. Electrocatalytic Reduction of CO2 and CO to Multi-Carbon Compounds over Cu-Based Catalysts. Chem. Soc. Rev. 2021, 50, 12897– 12914, DOI: 10.1039/D1CS00535A4https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXitFKqtLjK&md5=e6d0af591d622a59c47fffbfafb815cbElectrocatalytic reduction of CO2 and CO to multi-carbon compounds over Cu-based catalystsMa, Wenchao; He, Xiaoyang; Wang, Wei; Xie, Shunji; Zhang, Qinghong; Wang, YeChemical Society Reviews (2021), 50 (23), 12897-12914CODEN: CSRVBR; ISSN:0306-0012. (Royal Society of Chemistry)A review. The electrocatalytic redn. of CO2 with H2O to multi-carbon (C2+) compds., in particular, C2+ olefins and oxygenates, which have versatile applications in the chem. and energy industries, holds great potential to mitigate the depletion of fossil resources and abate carbon emissions. There are two major routes for the electrocatalytic CO2 redn. to C2+ compds., i.e., the direct route and the indirect route via CO. The electrocatalytic CO2 redn. to CO has been commercialised with solid oxide electrolyzers, making the indirect route via CO to C2+ compds. also a promising alternative. This tutorial review focuses on the similarities and differences in the electrocatalytic CO2 and CO redn. reactions (CO2RR and CORR) into C2+ compds., including C2H4, C2H5OH, CH3COO- and n-C3H7OH, over Cu-based catalysts. First, we introduce the fundamental aspects of the electrocatalytic reactions, including the cathode and anode reactions, electrocatalytic reactors and crucial performance parameters. Next, the reaction mechanisms, in particular, the C-C coupling mechanism, are discussed. Then, efficient catalysts and systems for these two reactions are critically reviewed. We analyze the key factors that det. the selectivity, activity and stability for the electrocatalytic CO2RR and CORR. Finally, the opportunities, challenges and future trends in the electrocatalytic CO2RR and CORR are proposed. These insights will offer guidance for the design of industrial-relevant catalysts and systems for the synthesis of C2+ olefins and oxygenates.
- 5Suominen, M.; Kallio, T. What we currently know about Carbon-Supported Metal and Metal Oxide Nanomaterials in Electrochemical CO2 Reduction. ChemElectroChem 2021, 8, 2397– 2406, DOI: 10.1002/celc.2021003455https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXhsVOmt7bN&md5=b4b203aad7f0ddd6d27942c0d3e13511What We Currently Know about Carbon-Supported Metal and Metal Oxide Nanomaterials in Electrochemical CO2 ReductionSuominen, Milla; Kallio, TanjaChemElectroChem (2021), 8 (13), 2397-2406CODEN: CHEMRA; ISSN:2196-0216. (Wiley-VCH Verlag GmbH & Co. KGaA)A review. Electrochem. redn. of CO2 is considered important in enhancing the circular-economy design; it can suppress harmful greenhouse-gas emissions while, combined with intermittent renewable energy sources, it can employ the surplus energy for prodn. of important chems. and fuels. In the process, electrocatalysts play an important role as the mediators of the highly active and selective conversion of CO2. Transition and post transition metals and their oxides are an important electrocatalyst group. For practical reasons, these metals need to be applied as nanoparticles supported on highly conducting materials enabling fabrication of 3D electrodes. In this mini, we focus on gathering our current knowledge on the effects which transition and post transition metal and metal oxide nanoparticles supported on different carbons may have on electrochem. redn. of CO2. We focus on literature of studies conducted in aq. conditions, under as similar conditions as possible, to ensure comparability. This approach enables us to highlight possible support effects and issues that complicate making conclusions on support effects.
- 6Wang, G.; Chen, J.; Ding, Y.; Cai, P.; Yi, L.; Li, Y.; Tu, C.; Hou, Y.; Wen, Z.; Dai, L. Electrocatalysis for CO2 Conversion: From Fundamentals to Value-Added Products. Chem. Soc. Rev. 2021, 50, 4993– 5061, DOI: 10.1039/D0CS00071J6https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXkvFKmt70%253D&md5=f43affba88dcc9183b0d298c53417079Electrocatalysis for CO2 conversion: from fundamentals to value-added productsWang, Genxiang; Chen, Junxiang; Ding, Yichun; Cai, Pingwei; Yi, Luocai; Li, Yan; Tu, Chaoyang; Hou, Yang; Wen, Zhenhai; Dai, LimingChemical Society Reviews (2021), 50 (8), 4993-5061CODEN: CSRVBR; ISSN:0306-0012. (Royal Society of Chemistry)A review. The continuously increasing CO2 released from human activities poses a great threat to human survival by fluctuating global climate and disturbing carbon balance among the four reservoirs of the biosphere, earth, air, and water. Converting CO2 to value-added feedstocks via electrocatalysis of the CO2 redn. reaction (CO2RR) has been regarded as one of the most attractive routes to re-balance the carbon cycle, thanks to its multiple advantages of mild operating conditions, easy handling, tunable products and the potential of synergy with the rapidly increasing renewable energy (i.e., solar, wind). Instead of focusing on a special topic of electrocatalysts for the CO2RR that have been extensively reviewed elsewhere, we herein present a rather comprehensive review of the recent research progress, in the view of assocd. value-added products upon selective electrocatalytic CO2 conversion. We initially provide an overview of the history and the fundamental science regarding the electrocatalytic CO2RR, with a special introduction to the design, prepn., and performance evaluation of electrocatalysts, the factors influencing the CO2RR, and the assocd. theor. calcns. Emphasis will then be given to the emerging trends of selective electrocatalytic conversion of CO2 into a variety of value-added products. The structure-performance relationship and mechanism will also be discussed and investigated. The outlooks for CO2 electrocatalysis, including the challenges and opportunities in the development of new electrocatalysts, electrolyzers, the recently rising operando fundamental studies, and the feasibility of industrial applications are finally summarized.
- 7Boutin, E.; Merakeb, L.; Ma, B.; Boudy, B.; Wang, M.; Bonin, J.; Anxolabéhère-Mallart, E.; Robert, M. Molecular Catalysis of CO2 reduction: Recent Advances and Perspectives in Electrochemical and Light-Driven Processes with Selected Fe, Ni and Co Aza Macrocyclic and Polypyridine Complexes. Chem. Soc. Rev. 2020, 49, 5772– 5809, DOI: 10.1039/D0CS00218F7https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXhsVags7rM&md5=13c4a6b0aabc350c8d040f22512aadc3Molecular catalysis of CO2 reduction: recent advances and perspectives in electrochemical and light-driven processes with selected Fe, Ni and Co aza macrocyclic and polypyridine complexesBoutin, E.; Merakeb, L.; Ma, B.; Boudy, B.; Wang, M.; Bonin, J.; Anxolabehere-Mallart, E.; Robert, M.Chemical Society Reviews (2020), 49 (16), 5772-5809CODEN: CSRVBR; ISSN:0306-0012. (Royal Society of Chemistry)A review. Earth-abundant Fe, Ni, and Co aza macrocyclic and polypyridine complexes have been thoroughly investigated for CO2 electrochem. and visible-light-driven redn. Since the first reports in the 1970s, an enormous body of work has been accumulated regarding the two-electron two-proton redn. of the gas, along with mechanistic and spectroscopic efforts to rationalize the reactivity and establish guidelines for structure-reactivity relationships. The ability to fine tune the ligand structure and the almost unlimited possibilities of designing new complexes have led to highly selective and efficient catalysts. Recent efforts toward developing hybrid systems upon combining mol. catalysts with conductive or semi-conductive materials have converged to high catalytic performances in water solns., to the inclusion of these catalysts into CO2 electrolyzers and photo-electrochem. devices, and to the discovery of catalytic pathways beyond two electrons. Combined with the continuous mechanistic efforts and new developments for in situ and in operando spectroscopic studies, mol. catalysis of CO2 redn. remains a highly creative approach.
- 8Azcarate, I.; Costentin, C.; Robert, M.; Savéant, J.-M. Through-Space Charge Interaction Substituent Effects in Molecular Catalysis Leading to the Design of the Most Efficient Catalyst of CO2-to-CO Electrochemical Conversion. J. Am. Chem. Soc. 2016, 138, 16639– 16644, DOI: 10.1021/jacs.6b070148https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XhvVCjsLbP&md5=783b8c66f38a6449af876b6931182c85Through-Space Charge Interaction Substituent Effects in Molecular Catalysis Leading to the Design of the Most Efficient Catalyst of CO2-to-CO Electrochemical ConversionAzcarate, Iban; Costentin, Cyrille; Robert, Marc; Saveant, Jean-MichelJournal of the American Chemical Society (2016), 138 (51), 16639-16644CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)The starting point of this study of through space-substituent effects on the catalysis of the electrochem. CO2-to-CO conversion by iron(0)-tetra-Ph porphyrins is the linear free energy correlation between through-structure electronic effects and the iron(I/0) std. potential established in ref. 1. The introduction of four pos. charged trimethylanilinium groups in para-position of the TPP phenyls results in an important pos. deviation from the correlation and a parallel improvement of the catalytic Tafel plot. The assignment of this catalysis boosting effect to the coulombic interaction of these pos. charges with the neg. charge borne by the initial Fe0-CO2 adduct is confirmed by the neg. deviation obsd. when the four pos. charges are replaced by four neg. charges borne by sulfonate groups also installed in the para-position of the TPP phenyls. The climax of this strategy of catalysis boosting by coulombic stabilization of the initial Fe0-CO2 adduct is reached when four pos. charged trimethylanilinium groups are introduced in ortho-position of the TPP phenyls. The addn. of a large concn. of a weak acid - phenol helps cleaving one of the C-O bonds of CO2. The efficiency of the resulting catalyst is unprecedented as can be judged by catalytic Tafel plot benchmarking with all presently available catalysts of the electrochem. CO2-to-CO conversion. The maximal turnover frequency is ≤106 s-1 and is reached at an overpotential of only 220 mV; the turnover frequency at zero overpotential is larger than 300 s-1. This catalyst leads to a highly selective formation of CO (practically 100%) in spite of the presence of a high concn. of phenol which could have favor H2 evolution. It is also very stable showing no significant alteration after more than eighty hours electrolysis.
- 9Monti, D.; Ottolina, G.; Carrea, G.; Riva, S. Redox Reactions Catalyzed by Isolated Enzymes. Chem. Rev. 2011, 111, 4111– 4140, DOI: 10.1021/cr100334x9https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC3MXltlaruro%253D&md5=e68132d4c7c6f44869a30763bbad722aRedox reactions catalyzed by isolated enzymesMonti, Daniela; Ottolina, Gianluca; Carrea, Giacomo; Riva, SergioChemical Reviews (Washington, DC, United States) (2011), 111 (7), 4111-4140CODEN: CHREAY; ISSN:0009-2665. (American Chemical Society)A review. The authors provide an overview of groups of oxidoreductases that are suitable for synthetic applications as isolated enzymes. The redox reactions catalyzed by these enzymes are numerous and varied. Included among the oxidoreductases discussed in detail are dehydrogenases, oxidases, oxygenases (including cytochromes P 450), and peroxidases.
- 10Meneghello, M.; Léger, C.; Fourmond, V. Electrochemical Studies of CO2-Reducing Metalloenzymes. Chem. – Eur. J. 2021, 27, 17542– 17553, DOI: 10.1002/chem.20210270210https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXitlams7zE&md5=819dcab4143e90872230ed6fd08b7d00Electrochemical Studies of CO2-Reducing MetalloenzymesMeneghello, Marta; Leger, Christophe; Fourmond, VincentChemistry - A European Journal (2021), 27 (70), 17542-17553CODEN: CEUJED; ISSN:0947-6539. (Wiley-VCH Verlag GmbH & Co. KGaA)A review. Only two enzymes are capable of directly reducing CO2: CO dehydrogenase, which produces CO at a [NiFe4S4] active site, and formate dehydrogenase, which produces formate at a mononuclear W or Mo active site. Both metalloenzymes are very rapid, energy-efficient and specific in terms of product. They have been connected to electrodes with two different objectives. A series of studies used protein film electrochem. to learn about different aspects of the mechanism of these enzymes (reactivity with substrates, inhibitors...). Another series focused on taking advantage of the catalytic performance of these enzymes to build biotechnol. devices, from CO2-reducing electrodes to full photochem. devices performing artificial photosynthesis. Here, we review all these works.
- 11Svetlitchnyi, V.; Peschel, C.; Acker, G.; Meyer, O. Two Membrane-Associated NiFeS-Carbon Monoxide Dehydrogenases from the Anaerobic Carbon-Monoxide-Utilizing Eubacterium Carboxydothermus Hydrogenoformans. J. Bacteriol. 2001, 183, 5134– 5144, DOI: 10.1128/JB.183.17.5134-5144.200111https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3MXmtFKrs7k%253D&md5=361f94957baba8c8d84676c377519affTwo membrane-associated NiFeS-carbon monoxide dehydrogenases from the anaerobic carbon-monoxide-utilizing eubacterium Carboxydothermus hydrogenoformansSvetlitchnyi, Vitali; Peschel, Christine; Acker, Georg; Meyer, OrtwinJournal of Bacteriology (2001), 183 (17), 5134-5144CODEN: JOBAAY; ISSN:0021-9193. (American Society for Microbiology)Two monofunctional NiFeS carbon monoxide (CO) dehydrogenases, designated CODH I and CODH II, were purified to homogeneity from the anaerobic CO-utilizing eubacterium Carboxydothermus hydrogenoformans. Both enzymes differ in their subunit mol. masses, N-terminal sequences, peptide maps, and immunol. reactivities. Immunogold labeling of ultrathin sections revealed both CODHs in assocn. with the inner aspect of the cytoplasmic membrane. Both enzymes catalyze the reaction CO + H2O → CO2 + 2 e- + 2 H+. Oxidized viologen dyes are effective electron acceptors. The specific enzyme activities were 15,756 (CODH I) and 13,828 (CODH II) μmol of CO oxidized min-1 mg-1 of protein (Me viologen, pH 8.0, 70°). The two enzymes oxidize CO very efficiently, as indicated by kcat/Km values at 70° of 1.3·109 M-1 CO s-1 (CODH I) and 1.7·109 M-1 CO s-1 (CODH II). The apparent Km values at pH 8.0 and 70° are 30 and 18 μM CO for CODH I and CODH II, resp. Acetyl CoA synthase activity is not assocd. with the enzymes. CODH I (125 kDa, 62.5-kDa subunit) and CODH II (129 kDa, 64.5-kDa subunit) are homodimers contg. 1.3 to 1.4 and 1.7 atoms of Ni, 20 to 22 and 20 to 24 atoms of Fe, and 22 and 19 atoms of acid-labile sulfur, resp. ESR (EPR) spectroscopy revealed signals indicative of [4Fe-4S] clusters. Ni was EPR silent under any conditions tested. It is proposed that CODH I is involved in energy generation and that CODH II serves in anabolic functions.
- 12Hille, R.; Dingwall, S.; Wilcoxen, J. The Aerobic CO Dehydrogenase from Oligotropha Carboxidovorans. J. Biol. Inorg. Chem. 2015, 20, 243– 251, DOI: 10.1007/s00775-014-1188-412https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXhsVeku7rM&md5=bb16ded2286301af4b96e9653c8e49f2The aerobic CO dehydrogenase from Oligotropha carboxidovoransHille, Russ; Dingwall, Stephanie; Wilcoxen, JarettJBIC, Journal of Biological Inorganic Chemistry (2015), 20 (2), 243-251CODEN: JJBCFA; ISSN:0949-8257. (Springer)A review. The authors review the recent literature dealing with Mo- and Cu-dependent carbon monoxide dehydrogenase of O. carboxidovorans, with particular emphasis on the structure of the enzyme and recent advances in the understanding of the enzyme catalytic mechanism.
- 13Can, M.; Armstrong, F. A.; Ragsdale, S. W. Structure, Function, and Mechanism of the Nickel Metalloenzymes, CO Dehydrogenase, and Acetyl-CoA Synthase. Chem. Rev. 2014, 114, 4149– 4174, DOI: 10.1021/cr400461p13https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC2cXisVWhtLo%253D&md5=e61881c21866dd429c6924d2d9f57335Structure, function, and mechanism of the nickel metalloenzymes, CO dehydrogenase, and acetyl-CoA synthaseCan, Mehmet; Armstrong, Fraser A.; Ragsdale, Stephen W.Chemical Reviews (Washington, DC, United States) (2014), 114 (8), 4149-4174CODEN: CHREAY; ISSN:0009-2665. (American Chemical Society)A review. There are 6 known pathways by which CO2 is fixed, with the Calvin cycle and photosynthesis providing most of the fixed carbon. Under anaerobic conditions, the Wood-Ljungdahl pathway is a predominant CO2 sink, and the Ni-contg. metalloenzymes, carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS), are the key enzymes in this pathway. Here, the structure, function, and catalytic mechanism of these 2 metalloenzymes, that have defined novel biochem. mechanisms involving organometallic chem. to catalyze their reactions, are discussed. CODH, esp. coupled to ACS and other enzymes of the Wood-Ljungdahl pathway, offers great potential for biotechnol. through the conversion of simple abundant compds. into needed chems. and fuels. Developing an industrial process that efficiently couples CO2 redn. to CO with a carbonylation reaction would be an important advance to the chem. industry because C-C bond formation by reactions with CO is instrumental in many industrial processes. CODH/ACS catalyze such a coupled process as an important component of the biol. carbon cycle. If fuels could be made from CO2, these C-C bond-forming reactions will be of even more importance in energy generation.
- 14Lindahl, P. A. The Ni-Containing Carbon Monoxide Dehydrogenase Family: Light at the End of the Tunnel?. Biochemistry 2002, 41, 2097– 2105, DOI: 10.1021/bi015932+14https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD38Xns1KhsA%253D%253D&md5=e8037b60c521ec0f02df429cc7a080dbThe Ni-Containing Carbon Monoxide Dehydrogenase Family: Light at the End of the Tunnel?Lindahl, Paul A.Biochemistry (2002), 41 (7), 2097-2105CODEN: BICHAW; ISSN:0006-2960. (American Chemical Society)A review on characterization, x-ray structure, and spectroscopic and redox properties of the Ni-contg. CO dehydrogenase (CODH) family of enzymes. The complexity and functional unity of the metal center structures, tunnels, and catalytic mechanisms employed by the CODH family of enzymes are discussed.
- 15Jeoung, J.-H.; Dobbek, H. Carbon Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide Dehydrogenase. Science 2007, 318, 1461– 1464, DOI: 10.1126/science.114848115https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD2sXhtlGmtLbO&md5=ced0378cfcee05f1b3aae1553acae5acCarbon Dioxide Activation at the Ni,Fe-Cluster of Anaerobic Carbon Monoxide DehydrogenaseJeoung, Jae-Hun; Dobbek, HolgerScience (Washington, DC, United States) (2007), 318 (5855), 1461-1464CODEN: SCIEAS; ISSN:0036-8075. (American Association for the Advancement of Science)Anaerobic CO dehydrogenases catalyze the reversible oxidn. of CO to CO2 at a complex Ni-, Fe-, and S-contg. metal center called cluster C. We report crystal structures of CO dehydrogenase II from Carboxydothermus hydrogenoformans in three different states. In a reduced state, exogenous CO2 supplied in soln. is bound and reductively activated by cluster C. In the intermediate structure, CO2 acts as a bridging ligand between Ni and the asym. coordinated Fe, where it completes the square-planar coordination of the Ni ion. It replaces a water/hydroxo ligand bound to the Fe ion in the other two states. The structures define the mechanism of CO oxidn. and CO2 redn. at the Ni-Fe site of cluster C.
- 16Contaldo, U.; Guigliarelli, B.; Perard, J.; Rinaldi, C.; Le Goff, A.; Cavazza, C. Efficient Electrochemical CO2/CO Interconversion by an Engineered Carbon Monoxide Dehydro-genase on a Gas-Diffusion Carbon Nanotube-Based Bioelectrode. ACS Catal. 2021, 11, 5808– 5817, DOI: 10.1021/acscatal.0c0543716https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXpsFGgsLk%253D&md5=057d0326e7144e3a2fbbd36aa063db03Efficient Electrochemical CO2/CO Interconversion by an Engineered Carbon Monoxide Dehydrogenase on a Gas-Diffusion Carbon Nanotube-Based BioelectrodeContaldo, Umberto; Guigliarelli, Bruno; Perard, Julien; Rinaldi, Clara; Le Goff, Alan; Cavazza, ChristineACS Catalysis (2021), 11 (9), 5808-5817CODEN: ACCACS; ISSN:2155-5435. (American Chemical Society)Carbon monoxide dehydrogenase catalyzes the reversible oxidn. of CO to CO2. The monofunctional enzyme from Rhodospirillum rubrum (RrCODH) has been extensively characterized in the past, although its use and investigation by bioelectrochem. have been limited. Here, we developed a heterologous system yielding a highly stable and active recombinant RrCODH in one-step purifn., with CO oxidn. activity reaching a max. of 26 500 U·mg-1, making RrCODH the most active CODH under ambient conditions described so far. ESR was used to precisely characterize the recombinant RrCODH, demonstrating the integrity of the active site. Selective CO2/CO interconversion with max. turnover frequencies of 150 s-1 for CO oxidn. (1.5 mA cm-2 at 250 mV overpotential) and 420 s-1 for CO2 redn. (4.2 mA cm-2 at 180 mV overpotential) is catalyzed by the recombinant RrCODH immobilized on MWCNT electrodes modified with 1-pyrenebutyric acid adamantyl amide (MWCNTADA), either in a classic three-electrode cell or in specifically designed CO2/CO-diffusing electrodes. This functional device is stable for hours with a turnover no. of at least 800 000. The performances of recombinant RrCODH-modified MWCNTADA are close to the best metal-based and mol.-based catalysts. These results greatly increase the benchmark for bioelectrocatalysis of reversible CO2 conversion.
- 17Dobbek, H.; Svetlitchnyi, V.; Gremer, L.; Huber, R.; Meyer, O. Crystal Structure of a Carbon Monoxide Dehydrogenase Reveals a Ni-4Fe-5S Cluster. Science 2001, 293, 1281– 1285, DOI: 10.1126/science.106150017https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3MXmtFCrtr4%253D&md5=72c4c709d2985f28dc7732c0b4c804e7Crystal structure of a carbon monoxide dehydrogenase reveals a [Ni-4Fe-5S] clusterDobbek, Holger; Svetlitchnyi, Vitali; Gremer, Lothar; Huber, Robert; Meyer, OrtwinScience (Washington, DC, United States) (2001), 293 (5533), 1281-1285CODEN: SCIEAS; ISSN:0036-8075. (American Association for the Advancement of Science)The homodimeric Ni-contg. carbon monoxide dehydrogenase (I) from the anaerobic bacterium, Carboxydothermus hydrogenoformans, catalyzes the oxidn. of CO to CO2. Here, the crystal structure of reduced I was solved at 1.6 Å resoln. This structure represents the prototype for Ni-contg. I from anaerobic bacteria and archae. I contained 5 metal clusters, of which clusters B, B', and a subunit-bridging, surface-exposed cluster D, were cubane-type [4Fe-4S] clusters. I active site clusters C and C' were novel, asym. [Ni-4Fe-5S] clusters. The integral Ni ion, which is the likely site of CO oxidn., was coordinated by 4 S ligands with square planar geometry.
- 18Contaldo, U.; Curtil, M.; Pérard, J.; Cavazza, C.; Le Goff, A. A Pyrene-Triazacyclononane Anchor Affords High Operational Stability for CO2 RR by a CNT-Supported Histidine-Tagged CODH. Angew. Chem., Int. Ed. 2022, e202117212 DOI: 10.1002/anie.20211721218https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB38XnvFajt78%253D&md5=ca6917011789f536edc1876d4f3ba256A Pyrene-Triazacyclononane Anchor Affords High Operational Stability for CO2RR by a CNT-Supported Histidine-Tagged CODHContaldo, Umberto; Curtil, Mathieu; Perard, Julien; Cavazza, Christine; Le Goff, AlanAngewandte Chemie, International Edition (2022), 61 (21), e202117212CODEN: ACIEF5; ISSN:1433-7851. (Wiley-VCH Verlag GmbH & Co. KGaA)An original 1-acetato-4-(1-pyrenyl)-1,4,7-triazacyclononane (AcPyTACN) was synthesized for the immobilization of a His-tagged recombinant CODH from Rhodospirillum rubrum (RrCODH) on carbon-nanotube electrodes. The strong binding of the enzyme at the Ni-AcPyTACN complex affords a high c.d. of 4.9 mA cm-2 towards electroenzymic CO2 redn. and a high stability of more than 6x106 TON when integrated on a gas-diffusion bioelectrode.
- 19Habermüller, K.; Mosbach, M.; Schuhmann, W. Electron-Transfer Mechanisms in Amperometric Biosensors. Fresenius’ J. Anal. Chem. 2000, 366, 560– 568, DOI: 10.1007/s00216005155119https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3cXhvF2lsr8%253D&md5=693c360d6d9f783fe808be972a53b5dfElectron-transfer mechanisms in amperometric biosensorsHabermuller, K.; Mosbach, M.; Schuhmann, W.Fresenius' Journal of Analytical Chemistry (2000), 366 (6-7), 560-568CODEN: FJACES; ISSN:0937-0633. (Springer-Verlag)Review with 156 refs. The function of amperometric biosensors is related to electron-transfer processes between the active site of an (immobilized) enzyme and an electrode surface which is poised to an appropriate working potential. Problems and specific features of architectures for amperometric biosensors using different electron-transfer pathways such as mediated electron transfer, electron-hopping in redox polymers, electron transfer using mediator-modified enzymes and carbon-paste electrodes, direct electron transfer by means of self-assembled monolayers or via conducting-polymer chains are discussed.
- 20Shin, W.; Lee, S. H.; Shin, J. W.; Lee, S. P.; Kim, Y. Highly Selective Electrocatalytic Conversion of CO2 to CO at −0.57 V (NHE) by Carbon Monoxide Dehydrogenase from Moorella Thermoacetica. J. Am. Chem. Soc. 2003, 125, 14688– 14689, DOI: 10.1021/ja037370i20https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD3sXovVCltrc%253D&md5=a924cfe05aaff5bc843f56a566a8f3faHighly Selective Electrocatalytic Conversion of CO2 to CO at -0.57 V (NHE) by Carbon Monoxide Dehydrogenase from Moorella thermoaceticaShin, Woonsup; Lee, Sang Hee; Shin, Jun Won; Lee, Sang Phil; Kim, YousungJournal of the American Chemical Society (2003), 125 (48), 14688-14689CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)We found that CODH is a fascinating enzyme for the electrochem. conversion of CO2 to CO. It could reduce CO2 to CO at -0.57 V vs. NHE with ∼100% current efficiency in 0.1 M phosphate buffer (pH 6.3). Nature's unique structure of C-cluster in CODH would be responsible for the low overpotential and the selective and fast conversion of CO2. The turnover no. per C-cluster is 700 h-1, and the pH optimum is 6.3.
- 21Schuhmann, W.; Wohlschläger, H.; Lammert, R.; Schmidt, H.-L.; Löffler, U.; Wiemhöfer, H.-D.; Göpel, W. Leaching of Dimethylferrocene, a Redox Mediator in Amperometric Enzyme Electrodes. Sens. Actuators, B 1990, 1, 571– 575, DOI: 10.1016/0925-4005(90)80275-5There is no corresponding record for this reference.
- 22Heller, A. Electron-Conducting Redox Hydrogels: Design, Characteristics and Synthesis. Curr. Opin. Chem. Biol. 2006, 10, 664– 672, DOI: 10.1016/j.cbpa.2006.09.01822https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD28Xht1Kgu7nN&md5=c643c609596159d0c91a5da79f7f5962Electron-conducting redox hydrogels: design, characteristics and synthesisHeller, AdamCurrent Opinion in Chemical Biology (2006), 10 (6), 664-672CODEN: COCBF4; ISSN:1367-5931. (Elsevier B.V.)A review. Redox hydrogels constitute the only electron-conducting phase in which water-sol. chems. and biochems. dissolve and diffuse. The combination of soly. and diffusion makes the electron-conducting gels permeable to water-sol. biochems. and chems. The electron-conducting redox hydrogels serve to elec. connect the redox centers of enzymes to electrodes, enabling their use whenever leaching of electron-shuttling diffusional redox mediators must be avoided, which is the case in s.c. implanted biosensors for diabetes management and in miniature, potentially implantable, glucose-O2 biofuel cells. Because the hydrogels envelope the redox enzymes, they elec. wire the reaction centers to electrodes irresp. of spatial orientation and connect to electrode redox centers of multiple enzyme layers. Hence, the attained current densities of enzyme substrate electrooxidn. or electroredn. are much higher than with enzyme monolayers packed onto electrode surfaces.
- 23Tapia, C.; Milton, R. D.; Pankratova, G.; Minteer, S. D.; Åkerlund, H.-E.; Leech, D.; De Lacey, A. L.; Pita, M.; Gorton, L. Wiring of Photosystem I and Hydrogenase on an Electrode for Photoelectrochemical H2 Production by Using Redox Polymers for Relatively Positive Onset Potential. ChemElectroChem 2017, 4, 90– 95, DOI: 10.1002/celc.20160050623https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC28XhsFymsLzO&md5=23e9cfdf9901b68a7c4962fdba0d00dbWiring of Photosystem I and Hydrogenase on an Electrode for Photoelectrochemical H2 Production by using Redox Polymers for Relatively Positive Onset PotentialTapia, Cristina; Milton, Ross D.; Pankratova, Galina; Minteer, Shelley D.; Aakerlund, Hans-Erik; Leech, Donal; De Lacey, Antonio L.; Pita, Marcos; Gorton, LoChemElectroChem (2017), 4 (1), 90-95CODEN: CHEMRA; ISSN:2196-0216. (Wiley-VCH Verlag GmbH & Co. KGaA)Photosystem I (PSI) is combined with Desulfovibrio gigas hydrogenase for the bioelectrocatalytic photosynthesis of hydrogen at an electrode surface. The activity of these two biocatalysts is linked by two redox polymers; a redox polymer with a relatively pos. potential (loaded with an Os complex) is able to reduce PSI and thus facilitates the prodn. of photoexcited electrons, whereas redox polymers of relatively low potential are able to transfer electrons to the hydrogenase. Two neg.-potential redox polymers are tested, with either a viologen pendant (4-methyl-4'-bromopropylviologen functionalized linear polyethylenimine) or a cobaltocene pendant (cobaltocene-functionalized branched polyethylenimine, Cc-BPEI). Both are able to protect hydrogenase from O2 inactivation, but only the use of Cc-BPEI yields significant photocurrents for H+ redn., likely due to its lower redox potential. The photocurrents obtained are found to be proportional to the quantity of H2 produced, reaching a max. of -30 μA cm-2 for the system incorporating Cc-BPEI and showing a relatively pos. onset potential at +0.38 V vs. SHE.
- 24Yuan, M.; Sahin, S.; Cai, R.; Abdellaoui, S.; Hickey, D. P.; Minteer, S. D.; Milton, R. D. Creating a Low-Potential Redox Polymer for Efficient Electroenzymatic CO2 Reduction. Angew. Chem., Int. Ed. 2018, 57, 6582– 6586, DOI: 10.1002/anie.20180339724https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXosFyis7c%253D&md5=3738a50cd73cc5a56551bf5304b34046Creating a Low-Potential Redox Polymer for Efficient Electroenzymatic CO2 ReductionYuan, Mengwei; Sahin, Selmihan; Cai, Rong; Abdellaoui, Sofiene; Hickey, David P.; Minteer, Shelley D.; Milton, Ross D.Angewandte Chemie, International Edition (2018), 57 (22), 6582-6586CODEN: ACIEF5; ISSN:1433-7851. (Wiley-VCH Verlag GmbH & Co. KGaA)Increasing greenhouse gas emissions have resulted in greater motivation to find novel carbon dioxide (CO2) redn. technologies, where the redn. of CO2 to valuable chem. commodities is desirable. Molybdenum-dependent formate dehydrogenase (Mo-FDH) from Escherichia coli is a metalloenzyme that is able to interconvert formate and CO2. We describe a low-potential redox polymer, synthesized by a facile method, that contains cobaltocene (grafted to poly(allylamine), Cc-PAA) to simultaneously mediate electrons to Mo-FDH and immobilize Mo-FDH at the surface of a carbon electrode. The resulting bioelectrode reduces CO2 to formate with a high Faradaic efficiency of 99±5 % at a mild applied potential of -0.66 V vs. SHE.
- 25So, K.; Sakai, K.; Kano, K. Gas Diffusion Bioelectrodes. Curr. Opin. Electrochem. 2017, 5, 173– 182, DOI: 10.1016/j.coelec.2017.09.00125https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1cXhtVGgsLfL&md5=e57c38d24b4c8a3d20a414c0ef53fc9bGas diffusion bioelectrodesSo, Keisei; Sakai, Kento; Kano, KenjiCurrent Opinion in Electrochemistry (2017), 5 (1), 173-182CODEN: COEUCY; ISSN:2451-9111. (Elsevier B.V.)A review. Currently, bioelectrocatalytic devices such as biofuel cells and bioreactors are recognized as new environment-friendly devices for the prodn. of electricity and valuable products. Thus far, systems have been improved from the viewpoints of enzymes and electrodes. A gas diffusion bioelectrode (GDBE) is one of the best approaches to improve electrode systems. This system has been remarkably developed and essentially employed in bioelectrocatalytic systems with gaseous substrates to realize high-speed H2 oxidn. and O2 redn. for biofuel cells and to realize the high-speed bioelectrocatalytic redn. of CO2. GDBEs permit the enzymes to directly use gaseous substrates, and it is imperative that the electrodes exhibit suitable porosity, cond., and hydrophobicity/hydrophilicity balance for the gas permeation and enzyme reaction at the bio-three-phase interface of GDBEs. In this review article, the major factors of GDBEs are discussed by highlighting recent remarkable contributions and challenges.
- 26Szczesny, J.; Birrell, J. A.; Conzuelo, F.; Lubitz, W.; Ruff, A.; Schuhmann, W. Redox-Polymer-Based High-Current-Density Gas-Diffusion H2-Oxidation Bioanode Using FeFe Hydrogenase from Desulfovibrio Desulfuricans in a Membrane-Free Biofuel Cell. Angew. Chem., Int. Ed. 2020, 59, 16506– 16510, DOI: 10.1002/anie.20200682426https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXhsVakur7J&md5=542ae01bb1ee951c068a19ef2a4a4143Redox-Polymer-Based High-Current-Density Gas-Diffusion H2-Oxidation Bioanode Using [FeFe] Hydrogenase from Desulfovibrio desulfuricans in a Membrane-free Biofuel CellSzczesny, Julian; Birrell, James A.; Conzuelo, Felipe; Lubitz, Wolfgang; Ruff, Adrian; Schuhmann, WolfgangAngewandte Chemie, International Edition (2020), 59 (38), 16506-16510CODEN: ACIEF5; ISSN:1433-7851. (Wiley-VCH Verlag GmbH & Co. KGaA)The incorporation of highly active but also highly sensitive catalysts (e.g. the [FeFe] hydrogenase from Desulfovibrio desulfuricans) in biofuel cells is still one of the major challenges in sustainable energy conversion. We report the fabrication of a dual-gas diffusion electrode H2/O2 biofuel cell equipped with a [FeFe] hydrogenase/redox polymer-based high-current-d. H2-oxidn. bioanode. The bioanodes show benchmark current densities of around 14 mA cm-2 and the corresponding fuel cell tests exhibit a benchmark for a hydrogenase/redox polymer-based biofuel cell with outstanding power densities of 5.4 mW cm-2 at 0.7 V cell voltage. Furthermore, the highly sensitive [FeFe] hydrogenase is protected against oxygen damage by the redox polymer and can function under 5 % O2.
- 27Lielpetere, A.; Becker, J. M.; Szczesny, J.; Conzuelo, F.; Ruff, A.; Birrell, J.; Lubitz, W.; Schuhmann, W. Enhancing the Catalytic Current Response of H2 Oxidation Gas Diffusion Bioelectrodes Using an Optimized Viologen-Based Redox Polymer and [NiFe] Hydrogenase. ELSA 2022, 2, e2100100 DOI: 10.1002/elsa.202100100There is no corresponding record for this reference.
- 28Ruff, A.; Szczesny, J.; Vega, M.; Zacarias, S.; Matias, P. M.; Gounel, S.; Mano, N.; Pereira, I. A. C.; Schuhmann, W. Redox-Polymer-Wired NiFeSe Hydrogenase Variants with Enhanced O2 Stability for Triple-Protected High-Current-Density H2-Oxidation Bioanodes. ChemSusChem 2020, 13, 3627– 3635, DOI: 10.1002/cssc.20200099928https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3cXhtFWlsLjN&md5=59543c3bae56f90b36d93dd98fd12b3fRedox-Polymer-Wired [NiFeSe] Hydrogenase Variants with Enhanced O2 Stability for Triple-Protected High-Current-Density H2-Oxidation BioanodesRuff, Adrian; Szczesny, Julian; Vega, Maria; Zacarias, Sonia; Matias, Pedro M.; Gounel, Sebastien; Mano, Nicolas; Pereira, Ines A. C.; Schuhmann, WolfgangChemSusChem (2020), 13 (14), 3627-3635CODEN: CHEMIZ; ISSN:1864-5631. (Wiley-VCH Verlag GmbH & Co. KGaA)Variants of the highly active [NiFeSe] hydrogenase from D. vulgaris Hildenborough that exhibit enhanced O2 tolerance were used as H2-oxidn. catalysts in H2/O2 biofuel cells. Two [NiFeSe] variants were elec. wired by means of low-potential viologen-modified redox polymers and evaluated with respect to H2-oxidn. and stability against O2 in the immobilized state. The two variants showed max. current densities of (450±84) μA cm-2 for G491A and (476±172) μA cm-2 for variant G941S on glassy carbon electrodes and a higher O2 tolerance than the wild type. In addn., the polymer protected the enzyme from O2 damage and high-potential inactivation, establishing a triple protection for the bioanode. The use of gas-diffusion bioanodes provided current densities for H2-oxidn. of up to 6.3 mA cm-2. Combination of the gas-diffusion bioanode with a bilirubin oxidase-based gas-diffusion O2-reducing biocathode in a membrane-free biofuel cell under anode-limiting conditions showed unprecedented benchmark power densities of 4.4 mW cm-2 at 0.7 V and an open-circuit voltage of 1.14 V even at moderate catalyst loadings, outperforming the previously reported system obtained with the [NiFeSe] wild type and the [NiFe] hydrogenase from D. vulgaris Miyazaki F.
- 29Szczesny, J.; Ruff, A.; Oliveira, A. R.; Pita, M.; Pereira, I. A. C.; de Lacey, A. L.; Schuhmann, W. Electroenzymatic CO2 Fixation Using Redox Polymer/Enzyme-Modified Gas Diffusion Electrodes. ACS Energy Lett. 2020, 5, 321– 327, DOI: 10.1021/acsenergylett.9b0243629https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BC1MXisVygt7vJ&md5=7aa761f577b595e421e3d689b9a0e574Electroenzymatic CO2 Fixation Using Redox Polymer/Enzyme-Modified Gas Diffusion ElectrodesSzczesny, Julian; Ruff, Adrian; Oliveira, Ana R.; Pita, Marcos; Pereira, Ines A. C.; De Lacey, Antonio L.; Schuhmann, WolfgangACS Energy Letters (2020), 5 (1), 321-327CODEN: AELCCP; ISSN:2380-8195. (American Chemical Society)The authors describe the fabrication of gas diffusion electrodes modified with polymer/enzyme layers for electroenzymic CO2 fixation. For this, a metal-free org. low-potential viologen-modified polymer was synthesized that reveals a redox potential of ∼-0.39 V vs. SHE and is thus able to elec. wire W-dependent formate dehydrogenase from Desulfovibrio vulgaris Hildenborough, which reversibly catalyzes the conversion of CO2 to formate. The use of gas diffusion electrodes eliminates limitations arising from slow mass transport when solid carbonate was used as CO2 source. The electrodes showed satisfactory stability that allowed for their long-term electrolysis application for electroenzymic formate prodn.
- 30Sehnal, D.; Bittrich, S.; Deshpande, M.; Svobodová, R.; Berka, K.; Bazgier, V.; Velankar, S.; Burley, S. K.; Koča, J.; Rose, A. S. Mol* Viewer: Modern Web App for 3D Visualization and Analysis of Large Biomolecular Structures. Nucleic Acids Res. 2021, 49, W431– W437, DOI: 10.1093/nar/gkab31430https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BB3MXhvV2isLbE&md5=ca2af5f4d0fa7758fcb0aaaf758790deMol* viewer: modern web app for 3D visualization and analysis of large biomolecular structuresSehnal, David; Bittrich, Sebastian; Deshpande, Mandar; Svobodova, Radka; Berka, Karel; Bazgier, Vaclav; Velankar, Sameer; Burley, Stephen K.; Koca, Jaroslav; Rose, Alexander S.Nucleic Acids Research (2021), 49 (W1), W431-W437CODEN: NARHAD; ISSN:1362-4962. (Oxford University Press)Large biomol. structures are being detd. exptl. on a daily basis using established techniques such as crystallog. and electron microscopy. In addn., emerging integrative or hybrid methods (I/HM) are producing structural models of huge macromol. machines and assemblies, sometimes contg. 100s of millions of non-hydrogen atoms. The performance requirements for visualization and anal. tools delivering these data are increasing rapidly. Significant progress in developing online, web-native three-dimensional (3D) visualization tools was previously accomplished with the introduction of the LiteMol suite and NGL Viewers. Thereafter, Mol* development was jointly initiated by PDBe and RCSB PDB to combine and build on the strengths of LiteMol (developed by PDBe) and NGL (developed by RCSB PDB). The web-native Mol* Viewer enables 3D visualization and streaming of macromol. coordinate and exptl. data, together with capabilities for displaying structure quality, functional, or biol. context annotations. High-performance graphics and data management allows users to simultaneously visualise up to hundreds of (superimposed) protein structures, stream mol. dynamics simulation trajectories, render cell-level models, or display huge I/HM structures. It is the primary 3D structure viewer used by PDBe and RCSB PDB. It can be easily integrated into third-party services.
- 31Dobbek, H.; Svetlitchnyi, V.; Liss, J.; Meyer, O. Carbon Monoxide Induced Decomposition of the Active Site Ni-4Fe-5S Cluster of CO Dehydrogenase. J. Am. Chem. Soc. 2004, 126, 5382– 5387, DOI: 10.1021/ja037776v31https://chemport.cas.org/services/resolver?origin=ACS&resolution=options&coi=1%3ACAS%3A528%3ADC%252BD2cXis1Cju7o%253D&md5=d9f6ccfac15712f1106df252645d60d0Carbon Monoxide Induced Decomposition of the Active Site [Ni-4Fe-5S] Cluster of CO DehydrogenaseDobbek, Holger; Svetlitchnyi, Vitali; Liss, Jago; Meyer, OrtwinJournal of the American Chemical Society (2004), 126 (17), 5382-5387CODEN: JACSAT; ISSN:0002-7863. (American Chemical Society)During the past two years, crystal structures of Cu- and Mo-contg. carbon monoxide dehydrogenases (CODHs) and Ni- and Fe-contg. CODHs have been reported. The active site of CODHs from anaerobic bacteria (cluster C) is composed of Ni, Fe, and S for which crystallog. studies of the enzymes from Carboxydothermus hydrogenoformans, Rhodospirillum rubrum, and Moorella thermoacetica revealed structural similarities in the overall protein fold but showed substantial differences in the essential Ni coordination environment. The [Ni-4Fe-5S] cluster C in the fully catalytically competent dithionite-reduced CODH II from C. hydrogenoformans (CODHIICh) at 1.6 Å resoln. contains a characteristic μ2-sulfido ligand between Ni and Fe1, resulting in a square-planar ligand arrangement with four S-ligands at the Ni ion. In contrast, the [Ni-4Fe-4S] clusters C in CO-treated CODH from R. rubrum resolved at 2.8 Å and in CO-treated acetyl-CoA synthase/CODH complex from M. thermoacetica at 2.2 and 1.9 Å resoln., resp., do not contain the μ2-sulfido ligand between Ni and Fe1 and display dissimilar geometries at the Ni ion. The [Ni-4Fe-4S] cluster is composed of a cubane [Ni-3Fe-4S] cluster linked to a mononuclear Fe site. The described coordination geometries of the Ni ion in the [Ni-4Fe-4S] cluster of R. rubrum and M. thermoacetica deviate from the square-planar ligand geometry in the [Ni-4Fe-5S] cluster C of CODHIICh. In addn., the latter was converted into a [Ni-4Fe-4S] cluster under specific conditions. The objective of this study was to elucidate the relationship between the structure of cluster C in CODHIICh and the functionality of the protein. The authors have detd. the CO oxidn. activity of CODHIICh under different conditions of crystn., prepd. crystals of the enzyme in the presence of dithiothreitol or dithionite as reducing agents under an atm. of N2 or CO, and solved the corresponding structures at 1.1 to 1.6 Å resolns. Fully active CODHIICh obtained after incubation of the enzyme with dithionite under N2 revealed the [Ni-4Fe-5S] cluster. Short treatment of the enzyme with CO in the presence of dithiothreitol resulted in a catalytically competent CODHIICh with a CO-reduced [Ni-4Fe-5S] cluster, but a prolonged treatment with CO caused the loss of CO-oxidizing activity and revealed a [Ni-4Fe-4S] cluster, which did not contain a μ2-S. These data suggest that the [Ni-4Fe-4S] cluster of CODHIICh is an inactivated decompn. product originating from the [Ni-4Fe-5S] cluster.
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The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acsami.2c09547.
Literature comparison; redox polymer characterization; gas chromatography setup and results; and voltammetric characterization before and after long-term measurement (PDF)
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