A redox cycle with complex II prioritizes sulfide quinone oxidoreductase-dependent H₂S oxidation.

ABSTRACT: The dual roles of H₂S as an endogenously synthesized respiratory substrate and as a toxin raise questions as to how it is cleared when the electron transport chain is inhibited. Sulfide quinone oxidoreductase (SQOR) catalyzes the first step in the mitochondrial H₂S oxidation pathway, using CoQ as an electron acceptor, and connects to the electron transport chain at the level of complex III. We have discovered that at high H₂S concentrations, which are known to inhibit complex IV, a new redox cycle is established between SQOR and complex II, operating in reverse. Under these conditions, the purine nucleotide cycle and the malate aspartate shuttle furnish fumarate, which supports complex II reversal and leads to succinate accumulation. Complex II knockdown in

SUBMITTER: Kumar R 

PROVIDER: S-EPMC8683732 | biostudies-literature | 2022 Jan

REPOSITORIES: biostudies-literature