Hydrogen sulfide bypasses the rate-limiting oxygen activation of heme oxygenase.

ABSTRACT: Discovery of unidentified protein functions is of biological importance because it often provides new paradigms for many research areas. Mammalian heme oxygenase (HO) enzyme catalyzes the O₂-dependent degradation of heme into carbon monoxide (CO), iron, and biliverdin through numerous reaction intermediates. Here, we report that H₂S, a gaseous signaling molecule, is part of a novel reaction pathway that drastically alters HO's products, reaction mechanism, and catalytic properties. Our prediction of this interplay is based on the unique reactivity of H₂S with one of the HO intermediates. We found that in the presence of H₂S, HO produces new linear tetrapyrroles, which we identified as isomers of sulfur-containing biliverdin (SBV), and that only H

SUBMITTER: Matsui T 

PROVIDER: S-EPMC6204905 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature