ArticleThe journal of physical chemistry. A2020
Energetics for Proton Reduction in FeFe Hydrogenase.
Article in The journal of physical chemistry. A, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 8 citations in OpenAlex.
- QM/MM Modeling of the Electronic Structure and Properties of the Fe-S Clusters inInorganic chemistry · 2026Article
- Computational Modeling and Experimental Approaches for Understanding the Mechanisms of [FeFe]-Hydrogenase.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved HJournal of the American Chemical Society · 2025Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant HChemical communications (Cambridge, England) · 2022Article
- Lewis acid protection turns cyanide containing [FeFe]-hydrogenase mimics into proton reduction catalysts.Dalton transactions (Cambridge, England : 2003) · 2022Article
- Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Review
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The energetics for proton reduction in FeFe-hydrogenase has been reinvestigated by theoretical modeling, in light of recent experiments. Two different mechanisms have been considered. In the first one, the bridging hydride position was blocked by the enzyme, which is the mechanism that has been supported by a recent spectroscopic study by Cramer et al. A major difficulty in the present study to agree with experimental energetics was to find the right position for the added proton in the first reduction step. It was eventually found that the best position was as a terminal hydride on the distal iron, which has not been suggested in any of the recent, experimentally based mechanisms. The lowest transition state was surprisingly found to be a bond formation between a proton on a cysteine and the terminal hydride. This type of TS is similar to the one for heterolytic H
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