Metal-ligand cooperativity in the soluble hydrogenase-1 from Pyrococcus furiosus.

ABSTRACT: Metal-ligand cooperativity is an essential feature of bioinorganic catalysis. The design principles of such cooperativity in metalloenzymes are underexplored, but are critical to understand for developing efficient catalysts designed with earth abundant metals for small molecule activation. The simple substrate requirements of reversible proton reduction by the [NiFe]-hydrogenases make them a model bioinorganic system. A highly conserved arginine residue (R355) directly above the exogenous ligand binding position of the [NiFe]-catalytic core is known to be essential for optimal function because mutation to a lysine results in lower catalytic rates. To expand on our studies of soluble hydrogenase-1 from Pyrococcus furiosus (Pf SH1), we investigated the role of R355 by site-dir

SUBMITTER: Vansuch GE 

PROVIDER: S-EPMC8163435 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature