ArticleThe Journal of biological chemistry2012
Importance of the protein framework for catalytic activity of [FeFe]-hydrogenases.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 150 citations in OpenAlex.
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- Segmented-overlap Fourier filtering and averaging (SOFFA) approach to improve concentration sensitivity of magnetic resonance spectra.Magnetic resonance (Gottingen, Germany) · 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
- Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase.ACS catalysis · 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
- Non-Covalent Integration of a [FeFe]-Hydrogenase Mimic to Multiwalled Carbon Nanotubes for Electrocatalytic Hydrogen Evolution.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022Article
- Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site.Chemical science · 2022Article
- 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
- Stability of the H-cluster under whole-cell conditions-formation of an HJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 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
- Supramolecular strategies in artificial photosynthesis.Chemical science · 2020Review
- Hydrogenase Mimics in MAngewandte Chemie (International ed. in English) · 2020Article
- Aromatic foldamers as scaffolds for metal second coordination sphere design.Chemical science · 2020Article
- Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture.Chemical science · 2020Article
- Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases.Journal of the American Chemical Society · 2020Article
- Electrochemical Characterization of a Complex FeFe Hydrogenase, the Electron-Bifurcating Hnd FromFrontiers in chemistry · 2020Article
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6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The active center (H-cluster) of [FeFe]-hydrogenases is embedded into a hydrophobic pocket within the protein. We analyzed several amino acids, located in the vicinity of this niche, by site-directed mutagenesis of the [FeFe]-hydrogenases from Clostridium pasteurianum (CpI) and Chlamydomonas reinhardtii (CrHydA1). These amino acids are highly conserved and predicted to be involved in H-cluster coordination. Characterization of two hydrogenase variants confirmed this hypothesis. The exchange of residues CrHydA1Met(415) and CrHydA1Lys(228) resulted in inactive proteins, which, according to EPR and FTIR analyses, contain no intact H-cluster. However, [FeFe]-hydrogenases in which CpIMet(353) (CrHydA1Met(223)) and CpICys(299) (CrHydA1Cys(169)) were exchanged to leucine and serine, respectively, showed a structurally intact H-cluster with catalytic activity either absent (CpIC299S) or strongly diminished (CpIM353L). In the case of CrHydA1C169S, the H-cluster was trapped in an inactive state exhibiting g values and vibrational frequencies that resembled the H(trans) state of DdH from Desulfovibrio desulfuricans. This cysteine residue, interacting with the bridge head nitrogen of the di(methyl)amine ligand, seems therefore to represent an essential contribution of the immediate protein environment to the reaction mechanism. Exchanging methionine CpIM(353) (CrHydA1M(223)) to leucine led to a strong decrease in turnover without affecting the K(m) value of the electron donor. We suggest that this methionine constitutes a "fine-tuning" element of hydrogenase activity.
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