Ontology highlight
ABSTRACT:
SUBMITTER: Winkler M
PROVIDER: S-EPMC5524980 | biostudies-literature | 2017 Jul
REPOSITORIES: biostudies-literature
Winkler Martin M Senger Moritz M Duan Jifu J Esselborn Julian J Wittkamp Florian F Hofmann Eckhard E Apfel Ulf-Peter UP Stripp Sven Timo ST Happe Thomas T
Nature communications 20170719
H<sub>2</sub> turnover at the [FeFe]-hydrogenase cofactor (H-cluster) is assumed to follow a reversible heterolytic mechanism, first yielding a proton and a hydrido-species which again is double-oxidized to release another proton. Three of the four presumed catalytic intermediates (H<sub>ox</sub>, H<sub>red</sub>/H<sub>red</sub> and H<sub>sred</sub>) were characterized, using various spectroscopic techniques. However, in catalytically active enzyme, the state containing the hydrido-species, whic ...[more]