Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe-S maturase proteins HydE, HydF, and HydG.

ABSTRACT: [FeFe] hydrogenases carry out the redox interconversion of protons and molecular hydrogen (2H⁺ + 2e^- ⇌ H₂) at a complex Fe-S active site known as the H-cluster. The H-cluster consists of a [4Fe-4S] subcluster, denoted here as [4Fe]_H, linked via a cysteine sulfur to an interesting organometallic [2Fe]_H subcluster thought to be the subsite where the catalysis occurs. This [2Fe]_H subcluster consists of two Fe atoms, linked with a bridging CO and a bridging SCH₂NHCH₂S azadithiolate (adt), with additional terminal CO and CN ligands bound to each Fe. Synthesizing such a complex organometallic unit is a fascinating problem in biochemistry, complicated by the toxic nature of both the CO and CN^-

SUBMITTER: Britt RD 

PROVIDER: S-EPMC8162317 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature