ArticleNature communications2015
Hydride bridge in [NiFe]-hydrogenase observed by nuclear resonance vibrational spectroscopy.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed.
- A Non-Covalent [4Fe-4S]/[2Fe] Interface in HydF Guides [FeFe]-Hydrogenase Maturation.Angewandte Chemie (International ed. in English) · 2026Article
- NRVS Spectroscopy Resolves Distinct Bridging Hydride Intermediates in [NiFe]-Hydrogenase.Journal of the American Chemical Society · 2025Article
- Practical issues in nuclear resonant vibrational spectroscopy for measuring biological samples: special problems, solutions and some perspectives.Applied spectroscopy reviews · 2025Article
- NRVS of FeS cluster proteins & models - A bestiary of nifty normal modes.Journal of inorganic biochemistry · 2025Review
- Article
- Nuclear resonant vibrational spectroscopy on Na-FeSpectroscopy letters; an international journal for rapid communication · 2025Article
- ATP-Triggered Fe(CN)Journal of the American Chemical Society · 2024Article
- Mechanistic Principles of Hydrogen Evolution in the Membrane-Bound Hydrogenase.Journal of the American Chemical Society · 2024Article
- X-ray and nuclear spectroscopies to reveal the element specific oxidation states and electronic spin states for nanoparticulated manganese cyanidoferrates and analogs.Physchem (Basel, Switzerland) · 2024Article
- Repurposing Iron- and 2-Oxoglutarate-Dependent Oxygenases to Catalyze Olefin Hydration.Angewandte Chemie (International ed. in English) · 2023Article
- Comprehensive structural, infrared spectroscopic and kinetic investigations of the roles of the active-site arginine in bidirectional hydrogen activation by the [NiFe]-hydrogenase 'Hyd-2' fromChemical science · 2023Article
- A personal account on 25 years of scientific literature on [FeFe]-hydrogenase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Review
- Stepwise assembly of the active site of [NiFe]-hydrogenase.Nature chemical biology · 2023Article
- Europium-151 and iron-57 nuclear resonant vibrational spectroscopy of naturally abundant KEu(III)Fe(II)(CN)Dalton transactions (Cambridge, England : 2003) · 2022Article
- 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 EChemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- The crystalline state as a dynamic system: IR microspectroscopy under electrochemical control for a [NiFe] hydrogenase.Chemical science · 2021Article
- HRSC advances · 2021Article
- Nuclear Resonance Vibrational Spectroscopy: A Modern Tool to Pinpoint Site-Specific Cooperative Processes.Crystals · 2021Article
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14 authors.
Funding
Abstract
The metabolism of many anaerobes relies on [NiFe]-hydrogenases, whose characterization when bound to substrates has proven non-trivial. Presented here is direct evidence for a hydride bridge in the active site of the (57)Fe-labelled fully reduced Ni-R form of Desulfovibrio vulgaris Miyazaki F [NiFe]-hydrogenase. A unique 'wagging' mode involving H(-) motion perpendicular to the Ni(μ-H)(57)Fe plane was studied using (57)Fe-specific nuclear resonance vibrational spectroscopy and density functional theory (DFT) calculations. On Ni(μ-D)(57)Fe deuteride substitution, this wagging causes a characteristic perturbation of Fe-CO/CN bands. Spectra have been interpreted by comparison with Ni(μ-H/D)(57)Fe enzyme mimics [(dppe)Ni(μ-pdt)(μ-H/D)(57)Fe(CO)3](+) and DFT calculations, which collectively indicate a low-spin Ni(II)(μ-H)Fe(II) core for Ni-R, with H(-) binding Ni more tightly than Fe. The present methodology is also relevant to characterizing Fe-H moieties in other important natural and synthetic catalysts.
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