Biosynthesis of the [FeFe] hydrogenase H-cluster via a synthetic [Fe(II)(CN)(CO)₂(cysteinate)]^- complex.

ABSTRACT: The H-cluster of [Fe-Fe] hydrogenase consists of a [4Fe]_H subcluster linked by the sulfur of a cysteine residue to an organometallic [2Fe]_H subcluster that utilizes terminal CO and CN ligands to each Fe along with a bridging CO and a bridging SCH₂NHCH₂S azadithiolate (adt) to catalyze proton reduction or hydrogen oxidation. Three Fe-S "maturase" proteins, HydE, HydF, and HydG, are responsible for the biosynthesis of the [2Fe]_H subcluster and its incorporation into the hydrogenase enzyme to form this catalytically active H-cluster. We have proposed that HydG is a bifunctional enzyme that uses S-adenosylmethione (SAM) bound to a [4Fe-4S] cluster to lyse tyrosine via a transient 5'-deoxyadenosyl radical

SUBMITTER: Britt RD 

PROVIDER: S-EPMC9175238 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature