Abstract Iron-sulfur (Fe/S) clusters are structurally and functionally diverse cofactors that are
found in all domains of life. 57 Fe Mössbauer spectroscopy is a technique that provides …

A novel in situ IR spectroscopic approach is demonstrated for the characterization of
hydrogenase during catalytic turnover. E. coli hydrogenase 1 (Hyd‐1) is adsorbed on a high …

Despite extensive studies on [NiFe]-hydrogenases, the mechanism by which these enzymes
produce and activate H2 so efficiently remains unclear. A well-known EPR-active state …

Purple bacteria are able to use H 2 for photoautotrophic, photomixotrophic, and
chemoautotrophic growth, exhibiting high metabolic lability. Depending on the type of …

The regulatory hydrogenase (RH) from Ralstonia eutropha H16 acts as a sensor for the
detection of environmental H2 and regulates gene expression related to hydrogenase …

Oxygen-tolerant [NiFe] hydrogenases are metalloenzymes that represent valuable model
systems for sustainable H2 oxidation and production. The soluble NAD+-reducing [NiFe] …

Hydrogenases are nature's catalysts designed to extract protons from molecular hydrogen
(H2) thereby forming a reactive hydride species (H−). Those enzymes capable of catalyzing …

We report the first direct electrochemical characterization of the impact of oxygen on the
hydrogen oxidation activity of an oxygen-tolerant, group 3, soluble [NiFe]-hydrogenase …

Protein immobilization on electrodes is a key concept in exploiting enzymatic processes for
bioelectronic devices. For optimum performance, an in-depth understanding of the enzyme …

We report here that a bioinspired cobalt diimine–dioxime molecular catalyst for hydrogen
evolution immobilized onto carbon nanotube electrodes proves tolerant toward oxygen. The …