Coordination chemistry controls the thiol oxidase activity of the B₁₂-trafficking protein CblC.

ABSTRACT: The cobalamin or B₁₂ cofactor supports sulfur and one-carbon metabolism and the catabolism of odd-chain fatty acids, branched-chain amino acids, and cholesterol. CblC is a B₁₂-processing enzyme involved in an early cytoplasmic step in the cofactor-trafficking pathway. It catalyzes the glutathione (GSH)-dependent dealkylation of alkylcobalamins and the reductive decyanation of cyanocobalamin. CblC from Caenorhabditis elegans (ceCblC) also exhibits a robust thiol oxidase activity, converting reduced GSH to oxidized GSSG with concomitant scrubbing of ambient dissolved O₂ The mechanism of thiol oxidation catalyzed by ceCblC is not known. In this study, we demonstrate that novel coordination chemistry accessible to ceCblC-bound cobala

SUBMITTER: Li Z 

PROVIDER: S-EPMC5465496 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature