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A personal account on 25 years of scientific literature on [FeFe]-hydrogenase

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Abstract

[FeFe]-hydrogenases are gas-processing metalloenzymes that catalyze H2 oxidation and proton reduction (H2 release) in microorganisms. Their high turnover frequencies and lack of electrical overpotential in the hydrogen conversion reaction has inspired generations of biologists, chemists, and physicists to explore the inner workings of [FeFe]-hydrogenase. Here, we revisit 25 years of scientific literature on [FeFe]-hydrogenase and propose a personal account on ‘must-read’ research papers and review article that will allow interested scientists to follow the recent discussions on catalytic mechanism, O2 sensitivity, and the in vivo synthesis of the active site cofactor with its biologically uncommon ligands carbon monoxide and cyanide. Focused on—but not restricted to—structural biology and molecular biophysics, we highlight future directions that may inspire young investigators to pursue a career in the exciting and competitive field of [FeFe]-hydrogenase research.

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Fig. 1

Reproduced with permission from the ACS

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Data availability

The datasets analysed during the current study are available from the corresponding authors on request.

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Acknowledgements

Sven T. Stripp is funded by the German Research Foundation (DFG) within the framework of SPP 1927 priority program “Iron-Sulfur for Life” (Grant No. STR1554/5-1). Jason W. Sidabras is funded by the Medical College of Wisconsin, while some results published in this work had funding from the European Union Horizon 2020 Marie Skłodowska-Curie Fellowship (no. 745702; ACT-EPR, https://act-epr.org) and the Max Planck Society.

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Sidabras, J.W., Stripp, S.T. A personal account on 25 years of scientific literature on [FeFe]-hydrogenase. J Biol Inorg Chem 28, 355–378 (2023). https://doi.org/10.1007/s00775-023-01992-5

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