A structural view of synthetic cofactor integration into [FeFe]-hydrogenases.

ABSTRACT: [FeFe]-hydrogenases are nature's fastest catalysts for the evolution or oxidation of hydrogen. Numerous synthetic model complexes for the [2Fe] subcluster (2Fe_H) of their active site are known, but so far none of these could compete with the enzymes. The complex Fe₂[μ-(SCH₂)₂X](CN)₂(CO)₄^2- with X = NH was shown to integrate into the apo-form of [FeFe]-hydrogenases to yield a fully active enzyme. Here we report the first crystal structures of the apo-form of the bacterial [FeFe]-hydrogenase CpI from Clostridium pasteurianum at 1.60 Å and the active semisynthetic enzyme, CpI^ADT, at 1.63 Å. The structures illustrate the significant changes in ligand coordination upon integration and activation of th

SUBMITTER: Esselborn J 

PROVIDER: S-EPMC5954619 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature