Quantum Chemical Study of a Radical Relay Mechanism for the HydG-Catalyzed Synthesis of a Fe(II)(CO)₂(CN)cysteine Precursor to the H-Cluster of [FeFe] Hydrogenase.

ABSTRACT: The [FeFe] hydrogenase catalyzes the redox interconversion of protons and H₂ with a Fe-S "H-cluster" employing CO, CN, and azadithiolate ligands to two Fe centers. The biosynthesis of the H-cluster is a highly interesting reaction carried out by a set of Fe-S maturase enzymes called HydE, HydF, and HydG. HydG, a member of the radical S-adenosylmethionine (rSAM) family, converts tyrosine, cysteine, and Fe(II) into an organometallic Fe(II)(CO)₂(CN)cysteine "synthon", which serves as the substrate for HydE. Although key aspects of the HydG mechanism have been experimentally determined via isotope-sensitive spectroscopic methods, other important mechanistic questions have eluded experimental determination. Here, we use computational quantum chemistry to refine the

SUBMITTER: Chen N 

PROVIDER: S-EPMC9649522 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature