ArticleThe journal of physical chemistry. B2022
Fast Proton Transport in FeFe Hydrogenase via a Flexible Channel and a Proton Hole Mechanism.
Article in The journal of physical chemistry. B, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 17 citations in OpenAlex.
- Proton Transfer Mechanisms in the MmpL3 Transporter ofACS bio & med chem Au · 2026Article
- NRVS of FeS cluster proteins & models - A bestiary of nifty normal modes.Journal of inorganic biochemistry · 2025Review
- Distinct Valence States of the [4Fe4S] Cluster Revealed in the Hydrogenase CrHydA1.Angewandte Chemie (International ed. in English) · 2025Article
- Predicting the Structure of Enzymes with Metal Cofactors: The Example of [FeFe] Hydrogenases.International journal of molecular sciences · 2024Article
- Phonon-assisted electron-proton transfer in [FeFe] hydrogenases: Topological role of clusters.Biophysical journal · 2023Article
- Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.Angewandte Chemie (International ed. in English) · 2023Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Di-iron hydrogenases are a class of enzymes that are capable of reducing protons to form molecular hydrogen with high efficiency. In addition to the catalytic site, these enzymes have evolved dedicated pathways to transport protons and electrons to the reaction center. Here, we present a detailed study of the most likely proton transfer pathway in such an enzyme using QM/MM molecular dynamics simulations. The protons are transported through a channel lined out from the protein exterior to the di-iron active site, by a series of hydrogen-bonded, weakly acidic or basic, amino acids and two incorporated water molecules. The channel shows remarkable flexibility, which is an essential feature to quickly reset the hydrogen-bond direction in the channel after each proton passing. Proton transport takes place via a "hole" mechanism, rather than an excess proton mechanism, the free energy landscape of which is remarkably flat, with a highest transition state barrier of only 5 kcal/mol. These results confirm our previous assumptions that proton transport is not rate limiting in the H
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