Cyanide-bridged iron complexes as biomimetics of tri-iron arrangements in maturases of the H cluster of the di-iron hydrogenase.

ABSTRACT: Developing from certain catalytic processes required for ancient life forms, the H₂ processing enzymes [NiFe]- and [FeFe]-hydrogenase (H₂ase) have active sites that are organometallic in composition, possessing carbon monoxide and cyanide as ligands. Simple synthetic analogues of the 2Fe portion of the active site of [FeFe]-H₂ase have been shown to dock into the empty carrier (maturation) protein, apo-Hyd-F, via the bridging ability of a terminal cyanide ligand from a low valent Fe^IFe^I unit to the iron of a 4Fe4S cluster of Hyd-F, with spectral evidence indicating CN isomerization during the coupling process (Berggren, et al., Nature, 2013, 499, 66-70). To probe the requirements for such cyanide couplings, w

SUBMITTER: Lunsford AM 

PROVIDER: S-EPMC6008931 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature