Cyanide Binding to [FeFe]-Hydrogenase Stabilizes the Alternative Configuration of the Proton Transfer Pathway.

ABSTRACT: Hydrogenases are H₂ converting enzymes that harbor catalytic cofactors in which iron (Fe) ions are coordinated by biologically unusual carbon monoxide (CO) and cyanide (CN^- ) ligands. Extrinsic CO and CN^- , however, inhibit hydrogenases. The mechanism by which CN^- binds to [FeFe]-hydrogenases is not known. Here, we obtained crystal structures of the CN^- -treated [FeFe]-hydrogenase CpI from Clostridium pasteurianum. The high resolution of 1.39 Å allowed us to distinguish intrinsic CN^- and CO ligands and to show that extrinsic CN^- binds to the open coordination site of the cofactor where CO is known to bind. In contrast to other inhibitors, CN^- treated crystals show conformational changes of conserved res

SUBMITTER: Duan J 

PROVIDER: S-EPMC10107461 | biostudies-literature | 2023 Feb

REPOSITORIES: biostudies-literature