When the inhibitor tells more than the substrate: the cyanide-bound state of a carbon monoxide dehydrogenase.

ABSTRACT: Carbon monoxide dehydrogenase (CODH) is a key enzyme for reversible CO interconversion. To elucidate structural and mechanistic details of CO binding at the CODH active site (C-cluster), cyanide is frequently used as an iso-electronic substitute and inhibitor. However, previous studies revealed conflicting results on the structure of the cyanide-bound complex and the mechanism of cyanide-inhibition. To address this issue in this work, we have employed IR spectroscopy, crystallography, site directed mutagenesis, and theoretical methods to analyse the cyanide complex of the CODH from Carboxydothermus hydrogenoformans (CODHII _Ch ). IR spectroscopy demonstrates that a single cyanide binds to the Ni ion. Whereas the inhibitor could be partially removed at elevated tempe

SUBMITTER: Ciaccafava A 

PROVIDER: S-EPMC6005268 | biostudies-literature | 2016 May

REPOSITORIES: biostudies-literature