ArticleProceedings of the National Academy of Sciences of the United States of America2016
Stepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamics.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. 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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Who cites it
20 citing papers in PubMed.
- Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase.ACS catalysis · 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
- Binding of exogenous cyanide reveals new active-site states in [FeFe] hydrogenases.Chemical science · 2023Article
- Molecular Basis of the Electron Bifurcation Mechanism in the [FeFe]-Hydrogenase Complex HydABC.Journal of the American Chemical Society · 2023Article
- Article
- Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.Angewandte Chemie (International ed. in English) · 2023Article
- 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
- Electrochemical control of [FeFe]-hydrogenase single crystals reveals complex redox populations at the catalytic site.Dalton transactions (Cambridge, England : 2003) · 2021Article
- Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies.Molecules (Basel, Switzerland) · 2021Review
- Two ligand-binding sites in CO-reducing V nitrogenase reveal a general mechanistic principle.Science advances · 2021Article
- [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Spin Polarization Reveals the Coordination Geometry of the [FeFe] Hydrogenase Active Site in Its CO-Inhibited State.The journal of physical chemistry letters · 2020Article
- How [FeFe]-Hydrogenase Facilitates Bidirectional Proton Transfer.Journal of the American Chemical Society · 2019Article
- The final steps of [FeFe]-hydrogenase maturation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases.Nature communications · 2018Article
- Spectroscopical Investigations on the Redox Chemistry of [FeFe]-Hydrogenases in the Presence of Carbon Monoxide.Molecules (Basel, Switzerland) · 2018Article
- Influence of the [4Fe-4S] cluster coordinating cysteines on active site maturation and catalytic properties ofChemical science · 2017Article
- Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis.The Journal of biological chemistry · 2017Article
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8 authors.
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Abstract
The six-iron cofactor of [FeFe]-hydrogenases (H-cluster) is the most efficient H2-forming catalyst in nature. It comprises a diiron active site with three carbon monoxide (CO) and two cyanide (CN(-)) ligands in the active oxidized state (Hox) and one additional CO ligand in the inhibited state (Hox-CO). The diatomic ligands are sensitive reporter groups for structural changes of the cofactor. Their vibrational dynamics were monitored by real-time attenuated total reflection Fourier-transform infrared spectroscopy. Combination of (13)CO gas exposure, blue or red light irradiation, and controlled hydration of three different [FeFe]-hydrogenase proteins produced 8 Hox and 16 Hox-CO species with all possible isotopic exchange patterns. Extensive density functional theory calculations revealed the vibrational mode couplings of the carbonyl ligands and uniquely assigned each infrared spectrum to a specific labeling pattern. For Hox-CO, agreement between experimental and calculated infrared frequencies improved by up to one order of magnitude for an apical CN(-) at the distal iron ion of the cofactor as opposed to an apical CO. For Hox, two equally probable isomers with partially rotated ligands were suggested. Interconversion between these structures implies dynamic ligand reorientation at the H-cluster. Our experimental protocol for site-selective (13)CO isotope editing combined with computational species assignment opens new perspectives for characterization of functional intermediates in the catalytic cycle.
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