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Electrocatalytic hydrogen oxidation by an enzyme at high carbon monoxide or oxygen levelsAnalyzing the catalytic processes of immobilized redox enzymes by vibrational spectroscopiesReversible [4Fe-3S] cluster morphing in an O(2)-tolerant [NiFe] hydrogenaseA unique iron-sulfur cluster is crucial for oxygen tolerance of a [NiFe]-hydrogenase.Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase.CO synthesized from the central one-carbon pool as source for the iron carbonyl in O2-tolerant [NiFe]-hydrogenase.Surface-enhanced vibrational spectroscopy for probing transient interactions of proteins with biomimetic interfaces: electric field effects on structure, dynamics and function of cytochrome c.Rubredoxin-related maturation factor guarantees metal cofactor integrity during aerobic biosynthesis of membrane-bound [NiFe] hydrogenaseInvestigation of the NADH/NAD(+) ratio in Ralstonia eutropha using the fluorescence reporter protein Peredox.Probing the origin of the metabolic precursor of the CO ligand in the catalytic center of [NiFe] hydrogenase.Spectroscopic Observation of Calcium-Induced Reorientation of Cellobiose Dehydrogenase Immobilized on Electrodes and its Effect on Electrocatalytic Activity.A universal scaffold for synthesis of the Fe(CN)2(CO) moiety of [NiFe] hydrogenase.Reversible active site sulfoxygenation can explain the oxygen tolerance of a NAD+-reducing [NiFe] hydrogenase and its unusual infrared spectroscopic properties.
P50
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P50
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Ingo Zebger
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