ArticleThe Journal of biological chemistry2011
Mechanism of proton transfer in [FeFe]-hydrogenase from Clostridium pasteurianum.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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46 citing papers in PubMed.
- Probing the Role of Accessory Domains in Oxygen Stability of [FeFe]-Hydrogenases.Journal of the American Chemical Society · 2026Article
- Probing the Role of Accessory FeS Clusters in Putative Sensory Group D [FeFe] Hydrogenase: Influence of the C-Terminal [4Fe-4S] Cluster on the Reactivity ofBiochemistry · 2026Article
- H-cluster Intermediates and Catalytic Properties ofBiochemistry · 2025Article
- Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved HJournal of the American Chemical Society · 2025Article
- Structural determinants of oxygen resistance and ZnProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Magnetotactic bacteria affiliated with diverse Pseudomonadota families biomineralize intracellular Ca-carbonate.The ISME journal · 2025Article
- Outer-sphere effects on the OChemical science · 2024Review
- Accessing a synthetic FeChemical science · 2024Article
- Kinetic Modeling of the Reversible or Irreversible Electrochemical Responses of FeFe-Hydrogenases.Journal of the American Chemical Society · 2024Article
- Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase.ACS catalysis · 2023Article
- Phonon-assisted electron-proton transfer in [FeFe] hydrogenases: Topological role of clusters.Biophysical journal · 2023Article
- Redox tuning of the H-cluster by second coordination sphere amino acids in the sensory [FeFe] hydrogenase fromChemical science · 2023Article
- Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases.Chemical science · 2023Article
- Radical Transport Facilitated by a Proton Transfer Network at the Subunit Interface of Ribonucleotide Reductase.Journal of the American Chemical Society · 2023Article
- Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.Angewandte Chemie (International ed. in English) · 2023Article
- Editorial: Hydrogenase: structure, function, maturation, and application.Frontiers in microbiology · 2023Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Fast Proton Transport in FeFe Hydrogenase via a Flexible Channel and a Proton Hole Mechanism.The journal of physical chemistry. B · 2022Article
- The Contribution of Proton-Donor pKa on Reactivity Profiles of [FeFe]-hydrogenases.Frontiers in microbiology · 2022Article
- Vibrational Perturbation of the [FeFe] Hydrogenase H-Cluster Revealed byJournal of the American Chemical Society · 2021Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
[FeFe]-Hydrogenases are complex metalloproteins that catalyze the reversible reduction of protons to molecular hydrogen utilizing a unique diiron subcluster bridged to a [4Fe4S] subcluster. Extensive studies have concentrated on the nature and catalytic activity of the active site, yet relatively little information is available concerning the mechanism of proton transport that is required for this activity. Previously, structural characterization of [FeFe]-hydrogenase from Clostridium pasteurianum indicated a potential proton transport pathway involving four residues (Cys-299, Glu-279, Ser-319, and Glu-282) that connect the active site to the enzyme surface. Here, we demonstrate that substitution of any of these residues resulted in a drastic reduction in hydrogenase activity relative to the native enzyme, supporting the importance of these residues in catalysis. Inhibition studies of native and amino acid-substituted enzymes revealed that Zn(2+) specifically blocked proton transfer by binding to Glu-282, confirming the role of this residue in the identified pathway. In addition, all four of these residues are strictly conserved, suggesting that they may form a proton transport pathway that is common to all [FeFe]-hydrogenases.
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