Nuclear resonance vibrational spectroscopy reveals the FeS cluster composition and active site vibrational properties of an O₂-tolerant NAD⁺-reducing [NiFe] hydrogenase.

ABSTRACT: Hydrogenases are complex metalloenzymes that catalyze the reversible splitting of molecular hydrogen into protons and electrons essentially without overpotential. The NAD⁺-reducing soluble hydrogenase (SH) from Ralstonia eutropha is capable of H₂ conversion even in the presence of usually toxic dioxygen. The molecular details of the underlying reactions are largely unknown, mainly because of limited knowledge of the structure and function the various metal cofactors present in the enzyme. Here all iron-containing cofactors of the SH were investigated by ⁵⁷Fe specific nuclear resonance vibrational spectroscopy (NRVS). Our data provide experimental evidence for one [2Fe2S] center and four [4Fe4S] clusters, which is consistent with amino acid sequence c

SUBMITTER: Lauterbach L 

PROVIDER: S-EPMC4321745 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature