Tuning Catalytic Bias of Hydrogen Gas Producing Hydrogenases.

ABSTRACT: Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions of the iron-sulfur-containing catalytic site with the local protein environment are thought to contribute to differences in catalytic reactivity, but this has not been demonstrated. The microbe Clostridium pasteurianum produces three [FeFe]-hydrogenases that differ in "catalytic bias" by exerting a disproportionate rate acceleration in one direction or the other that spans a remarkable 6 orders of magnitude. The combination of high-resolution structural work, biochemical analyses, and computational modeling indicates that protein secondary interactions directly influence the relative stabilization/destabilization of different oxidation states of the active

SUBMITTER: Artz JH 

PROVIDER: S-EPMC8653774 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature