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Engineering Thermostability in Artificial Metalloenzymes to Increase Catalytic Activity

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Download Hi-Res ImageDownload to MS-PowerPointCite This:ACS Catal. 2021, 11, 6, 3620-3627
    Research Article

    Engineering Thermostability in Artificial Metalloenzymes to Increase Catalytic Activity
    Click to copy article linkArticle link copied!

    • Megan V. Doble
      Megan V. Doble
      School of Chemistry, University of St Andrews, KY16 9ST St Andrews, U.K.
      More by Megan V. Doble
    • Lorenz Obrecht
      Lorenz Obrecht
      School of Chemistry, University of St Andrews, KY16 9ST St Andrews, U.K.
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    • Henk-Jan Joosten
      Henk-Jan Joosten
      Bio-Prodict, Nieuwe Marktstraat 54E, 6511 AA Nijmegen, The Netherlands
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    • Misun Lee
      Misun Lee
      Biotransformation and Biocatalysis, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
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    • Henriette J. Rozeboom
      Henriette J. Rozeboom
      Biotransformation and Biocatalysis, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
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    • Emma Branigan
      Emma Branigan
      School of Chemistry, University of St Andrews, KY16 9ST St Andrews, U.K.
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    • James. H. Naismith
      James. H. Naismith
      School of Chemistry, University of St Andrews, KY16 9ST St Andrews, U.K.
      Rosalind Franklin Institute, Harwell Campus, OX11 0FA Didcot, U.K.
      More by James. H. Naismith
      Orcidhttp://orcid.org/0000-0001-6744-5061
    • Dick B. Janssen
      Dick B. Janssen
      Biotransformation and Biocatalysis, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands
      More by Dick B. Janssen
      Orcidhttp://orcid.org/0000-0002-0834-2043
    • Amanda G. Jarvis*
      Amanda G. Jarvis
      School of Chemistry, University of St Andrews, KY16 9ST St Andrews, U.K.
      School of Chemistry, University of Edinburgh, Joseph Black Building, David Brewster Rd, Kings Buildings, EH9 3FJ Edinburgh, U.K.
      *Email: [email protected]
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      Orcidhttp://orcid.org/0000-0002-6414-0497
    • Paul C. J. Kamer
      Paul C. J. Kamer
      School of Chemistry, University of St Andrews, KY16 9ST St Andrews, U.K.
      Bioinspired Homo- & Heterogeneous Catalysis, Leibniz Institute for Catalysis, Albert-Einstein-Straße 29 a, Rostock 18059, Germany
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      Orcidhttp://orcid.org/0000-0002-9115-8844
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    ACS Catalysis

    Cite this: ACS Catal. 2021, 11, 6, 3620–3627
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acscatal.0c05413
    Published March 8, 2021
    Copyright © 2021 American Chemical Society
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    Abstract

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    Protein engineering has shown widespread use in improving the industrial application of enzymes and broadening the conditions they are able to operate under by increasing their thermostability and solvent tolerance. Here, we show that protein engineering can be used to increase the thermostability of an artificial metalloenzyme. Thermostable variants of the human steroid carrier protein 2L, modified to bind a metal catalyst, were created by rational design using structural data and a 3DM database. These variants were tested to identify mutations that enhanced the stability of the protein scaffold, and a significant increase in melting temperature was observed with a number of modified metalloenzymes. The ability to withstand higher reaction temperatures resulted in an increased activity in the hydroformylation of 1-octene, with more than fivefold improvement in turnover number, whereas the selectivity for linear aldehyde remained high up to 80%.

    Copyright © 2021 American Chemical Society

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    Supporting Information

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    Cited By

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    This article is cited by 22 publications.

    1. Jiamin Hu, Xiaoyu Chen, Lu Zhang, Jieyu Zhou, Guochao Xu, Ye Ni. Engineering the Thermostability of a d-Carbamoylase Based on Ancestral Sequence Reconstruction for the Efficient Synthesis of d-Tryptophan. Journal of Agricultural and Food Chemistry 2023, 71 (1) , 660-670. https://doi.org/10.1021/acs.jafc.2c07781
    2. Casey Van Stappen, Yunling Deng, Yiwei Liu, Hirbod Heidari, Jing-Xiang Wang, Yu Zhou, Aaron P. Ledray, Yi Lu. Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere. Chemical Reviews 2022, 122 (14) , 11974-12045. https://doi.org/10.1021/acs.chemrev.2c00106
    3. David A. Hueting, Sudarsana R. Vanga, Per-Olof Syrén. Thermoadaptation in an Ancestral Diterpene Cyclase by Altered Loop Stability. The Journal of Physical Chemistry B 2022, 126 (21) , 3809-3821. https://doi.org/10.1021/acs.jpcb.1c10605
    4. Alina Stein, Dongping Chen, Nico V. Igareta, Yoann Cotelle, Johannes G. Rebelein, Thomas R. Ward. A Dual Anchoring Strategy for the Directed Evolution of Improved Artificial Transfer Hydrogenases Based on Carbonic Anhydrase. ACS Central Science 2021, 7 (11) , 1874-1884. https://doi.org/10.1021/acscentsci.1c00825
    5. Yoshitsugu Morita, Hiroki Kubo, Ryusei Matsumoto, Nobutaka Fujieda. A thiopyridine-bound mirror-image copper center in an artificial non-heme metalloenzyme. Journal of Inorganic Biochemistry 2024, 260 , 112694. https://doi.org/10.1016/j.jinorgbio.2024.112694
    6. Samah Hashim Albayati, Nima Ghahremani Nezhad, Anmar Ghanim Taki, Raja Noor Zaliha Raja Abd Rahman. Efficient and easible biocatalysts: Strategies for enzyme improvement. A review. International Journal of Biological Macromolecules 2024, 276 , 133978. https://doi.org/10.1016/j.ijbiomac.2024.133978
    7. Dina Listov, Casper A. Goverde, Bruno E. Correia, Sarel Jacob Fleishman. Opportunities and challenges in design and optimization of protein function. Nature Reviews Molecular Cell Biology 2024, 25 (8) , 639-653. https://doi.org/10.1038/s41580-024-00718-y
    8. Zhi Zou, Bradley Higginson, Thomas R. Ward. Creation and optimization of artificial metalloenzymes: Harnessing the power of directed evolution and beyond. Chem 2024, 10 (8) , 2373-2389. https://doi.org/10.1016/j.chempr.2024.07.007
    9. Tao Wu, Yan Xu, Yao Nie, Xiaoqing Mu. Engineering the substrate acceptance of l-amine dehydrogenase enables the collective biocatalytic synthesis of N-heterocyclic primary amines. Chemical Engineering Journal 2024, 490 , 151735. https://doi.org/10.1016/j.cej.2024.151735
    10. E. Klemencic, R. C. Brewster, H. S. Ali, J. M. Richardson, A. G. Jarvis. Using BpyAla to generate copper artificial metalloenzymes: a catalytic and structural study. Catalysis Science & Technology 2024, 14 (6) , 1622-1632. https://doi.org/10.1039/D3CY01648J
    11. Jianzhong Sun, Xing He, Yilin LE, Rania Al-Tohamy, Sameh S. Ali. Potential applications of extremophilic bacteria in the bioremediation of extreme environments contaminated with heavy metals. Journal of Environmental Management 2024, 352 , 120081. https://doi.org/10.1016/j.jenvman.2024.120081
    12. Ritam Mukherjee, Manish Kumar Sah, Subhendu Dhibar, Ajaya Bhattarai, Bidyut Saha. Overview of homogeneous hydroformylation catalysis. 2024, 141-193. https://doi.org/10.1016/B978-0-443-15560-4.00003-4
    13. Shen‐Yuan Xu, Lei Zhou, Ying Xu, Han‐Yue Hong, Chen Dai, Ya‐Jun Wang, Yu‐Guo Zheng. Recent advances in structure‐based enzyme engineering for functional reconstruction. Biotechnology and Bioengineering 2023, 120 (12) , 3427-3445. https://doi.org/10.1002/bit.28540
    14. . In the Lab: Artificial Metalloenzymes for Sustainable Chemical Production : Johnson Matthey Technology Review features laboratory research. Johnson Matthey Technology Review 2023, 455-457. https://doi.org/10.1595/205651323X16923653528193
    15. Jie Luo, Chenshuo Song, Wenjing Cui, Laichuang Han, Zhemin Zhou. Counteraction of stability-activity trade-off of Nattokinase through flexible region shifting. Food Chemistry 2023, 423 , 136241. https://doi.org/10.1016/j.foodchem.2023.136241
    16. Ying Cai, Jin Zhou, Jianan Huang, Wenjuan Zhou, Yuting Wan, Martien A. Cohen Stuart, Junyou Wang. Rational design of polymeric nanozymes with robust catalytic performance via copper-ligand coordination. Journal of Colloid and Interface Science 2023, 645 , 458-465. https://doi.org/10.1016/j.jcis.2023.04.142
    17. Thomas Kuckhoff, Richard C. Brewster, Calum T. J. Ferguson, Amanda G. Jarvis. Reactivity Tuning of Metal‐Free Artificial Photoenzymes through Binding Site Specific Bioconjugation. European Journal of Organic Chemistry 2023, 26 (13) https://doi.org/10.1002/ejoc.202201412
    18. Zehua Zhang, Mengfei Long, Nan Zheng, Xiang Lü, Cailin Zhu, Tolbert Osire, Xiaole Xia, . Inside Out Computational Redesign of Cavities for Improving Thermostability and Catalytic Activity of Rhizomucor Miehei Lipase. Applied and Environmental Microbiology 2023, 89 (3) https://doi.org/10.1128/aem.02172-22
    19. Stefanie Hanreich, Elisa Bonandi, Ivana Drienovská. Design of Artificial Enzymes: Insights into Protein Scaffolds. ChemBioChem 2023, 24 (6) https://doi.org/10.1002/cbic.202200566
    20. Haoran Yu, Shuang Ma, Yiwen Li, Paul A. Dalby. Hot spots-making directed evolution easier. Biotechnology Advances 2022, 56 , 107926. https://doi.org/10.1016/j.biotechadv.2022.107926
    21. Claudèle Lemay-St-Denis, Nicolas Doucet, Joelle N Pelletier. Integrating dynamics into enzyme engineering. Protein Engineering, Design and Selection 2022, 35 https://doi.org/10.1093/protein/gzac015
    22. Soumyadeep Chakrabortty, Ahmad A. Almasalma, Johannes G. de Vries. Recent developments in asymmetric hydroformylation. Catalysis Science & Technology 2021, 11 (16) , 5388-5411. https://doi.org/10.1039/D1CY00737H
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    ACS Catalysis

    Cite this: ACS Catal. 2021, 11, 6, 3620–3627
    Click to copy citationCitation copied!
    https://doi.org/10.1021/acscatal.0c05413
    Published March 8, 2021
    Copyright © 2021 American Chemical Society
    Request reuse permissions

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