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Stepwise isotope editing of [FeFe]-hydrogenases exposes cofactor dynamicsIdentification of an Isothiocyanate on the HypEF Complex Suggests a Route for Efficient Cyanyl-Group Channeling during [NiFe]-Hydrogenase Cofactor GenerationThe influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation[NiFe]-hydrogenase maturation in vitro: analysis of the roles of the HybG and HypD accessory proteins1.The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia coli are iron- and carbon dioxide-binding proteins.[NiFe]-hydrogenase maturation: isolation of a HypC-HypD complex carrying diatomic CO and CN- ligands.The structure of the active site H-cluster of [FeFe] hydrogenase from the green alga Chlamydomonas reinhardtii studied by X-ray absorption spectroscopy.How oxygen attacks [FeFe] hydrogenases from photosynthetic organisms.How algae produce hydrogen--news from the photosynthetic hydrogenase.Surface-enhanced infrared absorption spectroscopy (SEIRAS) to probe monolayers of membrane proteins.Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases.Proteolytic cleavage orchestrates cofactor insertion and protein assembly in [NiFe]-hydrogenase biosynthesis.HypD is the scaffold protein for Fe-(CN)2CO cofactor assembly in [NiFe]-hydrogenase maturation.Immobilization of the [FeFe]-hydrogenase CrHydA1 on a gold electrode: design of a catalytic surface for the production of molecular hydrogen.Hydrogen and oxygen trapping at the H-cluster of [FeFe]-hydrogenase revealed by site-selective spectroscopy and QM/MM calculations.Protonation/reduction dynamics at the [4Fe-4S] cluster of the hydrogen-forming cofactor in [FeFe]-hydrogenases.Bridging Hydride at Reduced H-Cluster Species in [FeFe]-Hydrogenases Revealed by Infrared Spectroscopy, Isotope Editing, and Quantum Chemistry.The reductive phase of Rhodobacter sphaeroides cytochrome c oxidase disentangled by CO ligation.Proton-Coupled Reduction of the Catalytic [4Fe-4S] Cluster in [FeFe]-Hydrogenases.[FeFe]-Hydrogenases: recent developments and future perspectives.Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenasesThe [FeFe]-hydrogenase maturation protein HydF contains a H-cluster like [4Fe4S]-2Fe siteFormaldehyde--a rapid and reversible inhibitor of hydrogen production by [FeFe]-hydrogenasesSpectroscopical Investigations on the Redox Chemistry of [FeFe]-Hydrogenases in the Presence of Carbon MonoxideDiscovery of novel [FeFe]-hydrogenases for biocatalytic H2-productionThe Molecular Proceedings of Biological Hydrogen TurnoverHow [FeFe]-Hydrogenase Facilitates Bidirectional Proton TransferDifferential Protonation at the Catalytic Six-Iron Cofactor of [FeFe]-Hydrogenases Revealed by 57Fe Nuclear Resonance X-ray Scattering and Quantum Mechanics/Molecular Mechanics Analyses
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P50
description
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Sven T Stripp
@ast
Sven T Stripp
@en
Sven T Stripp
@es
Sven T Stripp
@nl
type
label
Sven T Stripp
@ast
Sven T Stripp
@en
Sven T Stripp
@es
Sven T Stripp
@nl
prefLabel
Sven T Stripp
@ast
Sven T Stripp
@en
Sven T Stripp
@es
Sven T Stripp
@nl
P106
P31
P496
0000-0002-8412-0258