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RETURN TO ISSUEPREVB: Biophysics; Physi...B: Biophysics; Physical Chemistry of Biological Systems and BiomoleculesNEXT

The Laser-Induced Potential Jump: A Method for Rapid Electron Injection into Oxidoreductase Enzymes

Cite this: J. Phys. Chem. B 2020, 124, 40, 8750–8760
Publication Date (Web):September 14, 2020
https://doi.org/10.1021/acs.jpcb.0c05718
Copyright © 2020 American Chemical Society

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    Abstract

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    Oxidoreductase enzymes often perform technologically useful chemical transformations using abundant metal cofactors with high efficiency under ambient conditions. The understanding of the catalytic mechanism of these enzymes is, however, highly dependent on the availability of well-characterized and optimized time-resolved analytical techniques. We have developed an approach for rapidly injecting electrons into a catalytic system using a photoactivated nanomaterial in combination with a range of redox mediators to produce a potential jump in solution, which then initiates turnover via electron transfer (ET) to the catalyst. The ET events at the nanomaterial-mediator-catalyst interfaces are, however, highly sensitive to the experimental conditions such as photon flux, relative concentrations of system components, and pH. Here, we present a systematic optimization of these experimental parameters for a specific catalytic system, namely, [FeFe] hydrogenase from Chlamydomonas reinhardtii (CrHydA1). The developed strategies can, however, be applied in the study of a wide variety of oxidoreductase enzymes. Our potential jump system consists of CdSe/CdS core–shell nanorods as a photosensitizer and a series of substituted bipyridinium salts as mediators with redox potentials in the range from −550 to −670 mV (vs SHE). With these components, we screened the effect of pH, mediator concentration, protein concentration, photosensitizer concentration, and photon flux on steady-state photoreduction and hydrogen production as well as ET and potential jump efficiency. By manipulating these experimental conditions, we show the potential of simple modifications to improve the tunability of the potential jump for application to study oxidoreductases.

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    The Supporting Information is available free of charge at https://pubs.acs.org/doi/10.1021/acs.jpcb.0c05718.

    • Material characterization, quantum efficiency of photodriven mediator reduction, steady-state solution potential during hydrogen production, fit coefficients for TCSPC data, data analysis for TR-Vis measurements, analysis of laser induced potential jump; fit coefficients for TR-Vis and TR-IR data, and proposed catalytic cycle for [FeFe] hydrogenase (PDF)

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    Cited By

    This article is cited by 8 publications.

    1. Mariia V. Pavliuk, Marco Lorenzi, Dustin R. Morado, Lars Gedda, Sina Wrede, Sara H. Mejias, Aijie Liu, Moritz Senger, Starla Glover, Katarina Edwards, Gustav Berggren, Haining Tian. Polymer Dots as Photoactive Membrane Vesicles for [FeFe]-Hydrogenase Self-Assembly and Solar-Driven Hydrogen Evolution. Journal of the American Chemical Society 2022, 144 (30) , 13600-13611. https://doi.org/10.1021/jacs.2c03882
    2. Monica L. K. Sanchez, Seth Wiley, Edward Reijerse, Wolfgang Lubitz, James A. Birrell, R. Brian Dyer. Time-Resolved Infrared Spectroscopy Reveals the pH-Independence of the First Electron Transfer Step in the [FeFe] Hydrogenase Catalytic Cycle. The Journal of Physical Chemistry Letters 2022, 13 (25) , 5986-5990. https://doi.org/10.1021/acs.jpclett.2c01467
    3. David W. White, Daniel Esckilsen, Seung Kyu Lee, Stephen W. Ragsdale, R. Brian Dyer. Efficient, Light-Driven Reduction of CO2 to CO by a Carbon Monoxide Dehydrogenase–CdSe/CdS Nanorod Photosystem. The Journal of Physical Chemistry Letters 2022, 13 (24) , 5553-5556. https://doi.org/10.1021/acs.jpclett.2c01412
    4. Sven T. Stripp. In Situ Infrared Spectroscopy for the Analysis of Gas-processing Metalloenzymes. ACS Catalysis 2021, 11 (13) , 7845-7862. https://doi.org/10.1021/acscatal.1c00218
    5. Jason W. Sidabras, Sven T. Stripp. A personal account on 25 years of scientific literature on [FeFe]-hydrogenase. JBIC Journal of Biological Inorganic Chemistry 2023, 28 (4) , 355-378. https://doi.org/10.1007/s00775-023-01992-5
    6. Solomon L. D. Wrathall, Barbara Procacci, Marius Horch, Emily Saxton, Chris Furlan, Julia Walton, Yvonne Rippers, James N. Blaza, Gregory M. Greetham, Michael Towrie, Anthony W. Parker, Jason Lynam, Alison Parkin, Neil T. Hunt. Ultrafast 2D-IR spectroscopy of [NiFe] hydrogenase from E. coli reveals the role of the protein scaffold in controlling the active site environment. Physical Chemistry Chemical Physics 2022, 24 (40) , 24767-24783. https://doi.org/10.1039/D2CP04188J
    7. Artavazd Badalyan, Zhi-Yong Yang, Maowei Hu, T. Leo Liu, Lance C. Seefeldt. Tailoring electron transfer pathway for photocatalytic N 2 -to-NH 3 reduction in a CdS quantum dots-nitrogenase system. Sustainable Energy & Fuels 2022, 6 (9) , 2256-2263. https://doi.org/10.1039/D2SE00148A
    8. James A. Birrell, Patricia Rodríguez-Maciá, Edward J. Reijerse, Maria Alessandra Martini, Wolfgang Lubitz. The catalytic cycle of [FeFe] hydrogenase: A tale of two sites. Coordination Chemistry Reviews 2021, 449 , 214191. https://doi.org/10.1016/j.ccr.2021.214191