HydE Catalytic Mechanism Is Powered by a Radical Relay with Redox-Active Fe(I)-Containing Intermediates.

ABSTRACT: [FeFe]-hydrogenases are enzymes that catalyze the redox interconversion of H⁺ and H₂ using a six-iron active site, known as the H-cluster, which consists of a structurally unique [2Fe]_H subcluster linked to a [4Fe-4S]_H subcluster. A set of enzymes, HydG, HydE, and HydF, are responsible for the biosynthesis of the [2Fe]_H subcluster. Among them, it is well established that HydG cleaves tyrosine into CO and CN^- and forms a mononuclear [Fe(II)(Cys)(CO)₂(CN)] complex. Recent work using EPR spectroscopy and X-ray crystallography show that HydE uses this organometallic Fe complex as its native substrate. The low spin Fe(II) center is reduced into an adenosylated Fe(I) species, which is proposed to fo

SUBMITTER: Chen N 

PROVIDER: S-EPMC11826987 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature