Structural characterization of HypX responsible for CO biosynthesis in the maturation of NiFe-hydrogenase.

ABSTRACT: Several accessory proteins are required for the assembly of the metal centers in hydrogenases. In NiFe-hydrogenases, CO and CN^- are coordinated to the Fe in the NiFe dinuclear cluster of the active center. Though these diatomic ligands are biosynthesized enzymatically, detail mechanisms of their biosynthesis remain unclear. Here, we report the structural characterization of HypX responsible for CO biosynthesis to assemble the active site of NiFe hydrogenase. CoA is constitutionally bound in HypX. Structural characterization of HypX suggests that the formyl-group transfer will take place from N¹⁰-formyl-THF to CoA to form formyl-CoA in the N-terminal domain of HypX, followed by decarbonylation of formyl-CoA to produce CO in the C-terminal domain though the direct exper

SUBMITTER: Muraki N 

PROVIDER: S-EPMC6802093 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature