Ontology highlight
ABSTRACT:
SUBMITTER: Nemeth B
PROVIDER: S-EPMC7399679 | biostudies-literature | 2020 Aug
REPOSITORIES: biostudies-literature
Németh Brigitta B Senger Moritz M Redman Holly J HJ Ceccaldi Pierre P Broderick Joan J Magnuson Ann A Stripp Sven T ST Haumann Michael M Berggren Gustav G
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 20200713 5
[FeFe]-hydrogenase enzymes employ a unique organometallic cofactor for efficient and reversible hydrogen conversion. This so-called H-cluster consists of a [4Fe-4S] cubane cysteine linked to a diiron complex coordinated by carbon monoxide and cyanide ligands and an azadithiolate ligand (adt = NH(CH<sub>2</sub>S)<sub>2</sub>)·[FeFe]-hydrogenase apo-protein binding only the [4Fe-4S] sub-complex can be fully activated in vitro by the addition of a synthetic diiron site precursor complex ([2Fe]<sup> ...[more]