Ontology highlight
ABSTRACT:
SUBMITTER: Senger M
PROVIDER: S-EPMC6823627 | biostudies-literature | 2019 Oct
REPOSITORIES: biostudies-literature
Senger Moritz M Eichmann Viktor V Laun Konstantin K Duan Jifu J Wittkamp Florian F Knör Günther G Apfel Ulf-Peter UP Happe Thomas T Winkler Martin M Heberle Joachim J Stripp Sven Timo ST
Journal of the American Chemical Society 20191015 43
Hydrogenases are metalloenzymes that catalyze the conversion of protons and molecular hydrogen, H<sub>2</sub>. [FeFe]-hydrogenases show particularly high rates of hydrogen turnover and have inspired numerous compounds for biomimetic H<sub>2</sub> production. Two decades of research on the active site cofactor of [FeFe]-hydrogenases have put forward multiple models of the catalytic proceedings. In comparison, our understanding of proton transfer is poor. Previously, residues were identified formi ...[more]