The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions.

ABSTRACT: [FeFe] hydrogenases have attracted extensive attention in the field of renewable energy research because of their remarkable efficiency for H₂ gas production. H₂ formation is catalyzed by a biologically unique hexanuclear iron cofactor denoted the H-cluster. The assembly of this cofactor requires a dedicated maturation machinery including HydF, a multidomain [4Fe4S] cluster protein with GTPase activity. HydF is responsible for harboring and delivering a precatalyst to the apo-hydrogenase, but the details of this process are not well understood. Here, we utilize gas-phase electrophoretic macromolecule analysis to show that a HydF dimer forms a transient interaction complex with the hydrogenase and that the formation of this complex depends on the cofactor content on Hy

SUBMITTER: Nemeth B 

PROVIDER: S-EPMC7450098 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature