ArticleAngewandte Chemie (International ed. in English)2018
Terminal Hydride Species in [FeFe]-Hydrogenases Are Vibrationally Coupled to the Active Site Environment.
Article in Angewandte Chemie (International ed. in English), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 32 citations in OpenAlex.
- QM/MM Modeling of the Electronic Structure and Properties of the Fe-S Clusters inInorganic chemistry · 2026Article
- Practical issues in nuclear resonant vibrational spectroscopy for measuring biological samples: special problems, solutions and some perspectives.Applied spectroscopy reviews · 2025Article
- H-cluster Intermediates and Catalytic Properties ofBiochemistry · 2025Article
- Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases.Chemical science · 2023Article
- Second and Outer Coordination Sphere Effects in Nitrogenase, Hydrogenase, Formate Dehydrogenase, and CO Dehydrogenase.Chemical reviews · 2022Review
- Machine learning concept in de-spiking process for nuclear resonant vibrational spectra - automation using no external parameter.Vibrational Spectroscopy · 2022Article
- The Contribution of Proton-Donor pKa on Reactivity Profiles of [FeFe]-hydrogenases.Frontiers in microbiology · 2022Article
- The EChemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- The Nonphysiological Reductant Sodium Dithionite and [FeFe] Hydrogenase: Influence on the Enzyme Mechanism.Journal of the American Chemical Society · 2021Article
- Nuclear Resonance Vibrational Spectroscopy: A Modern Tool to Pinpoint Site-Specific Cooperative Processes.Crystals · 2021Article
- Vibrational Perturbation of the [FeFe] Hydrogenase H-Cluster Revealed byJournal of the American Chemical Society · 2021Article
- High-Frequency Fe-H and Fe-HInorganic chemistry · 2021Article
- Energetics for Proton Reduction in FeFe Hydrogenase.The journal of physical chemistry. A · 2020Article
- Metal-ligand cooperativity in the soluble hydrogenase-1 fromChemical science · 2020Article
- Vibrational characterization of a diiron bridging hydride complex - a model for hydrogen catalysis.Chemical science · 2020Article
- Spectroscopic investigations under whole-cell conditions provide new insight into the metal hydride chemistry of [FeFe]-hydrogenase.Chemical science · 2020Article
- Spectroscopic and Computational Evidence that [FeFe] Hydrogenases Operate Exclusively with CO-Bridged Intermediates.Journal of the American Chemical Society · 2020Article
- Integrated bio-metal science: New frontiers of bio-metal science opened with cutting-edge techniques.Biophysics and physicobiology · 2020Article
- Asymmetry in the Ligand Coordination Sphere of the [FeFe] Hydrogenase Active Site Is Reflected in the Magnetic Spin Interactions of the Aza-propanedithiolate Ligand.The journal of physical chemistry letters · 2019Article
- Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases.Nature communications · 2018Article
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Authors and funding
13 authors at 5 institutions in 3 countries.
Funding
Abstract
A combination of nuclear resonance vibrational spectroscopy (NRVS), FTIR spectroscopy, and DFT calculations was used to observe and characterize Fe-H/D bending modes in CrHydA1 [FeFe]-hydrogenase Cys-to-Ser variant C169S. Mutagenesis of cysteine to serine at position 169 changes the functional group adjacent to the H-cluster from a -SH to -OH, thus altering the proton transfer pathway. The catalytic activity of C169S is significantly reduced compared to that of native CrHydA1, presumably owing to less efficient proton transfer to the H-cluster. This mutation enabled effective capture of a hydride/deuteride intermediate and facilitated direct detection of the Fe-H/D normal modes. We observed a significant shift to higher frequency in an Fe-H bending mode of the C169S variant, as compared to previous findings with reconstituted native and oxadithiolate (ODT)-substituted CrHydA1. On the basis of DFT calculations, we propose that this shift is caused by the stronger interaction of the -OH group of C169S with the bridgehead -NH- moiety of the active site, as compared to that of the -SH group of C169 in the native enzyme.
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