H₂O₂-Mediated Oxidative Stress Enhances Cystathionine γ-Lyase-Derived H₂S Synthesis via a Sulfenic Acid Intermediate.

ABSTRACT: Hydrogen sulfide (H₂S), which is generated mainly by cystathionine γ-lyase (CSE) in the cardiovascular system, plays a pivotal role in a wide range of physiological and pathological processes. However, the regulatory mechanism of the CSE/H₂S system is poorly understood. Herein, we show that oxidation induces the disulfide bond formation between Cys252 and Cys255 in the CXXC motif, thus stimulating the H₂S-producing activity of CSE. The activity of oxidized CSE is approximately 2.5 fold greater than that of the reduced enzyme. Molecular dynamics and molecular docking suggest that the disulfide bond formation induces the conformational change in the active site of CSE and consequently increases the affinity of the enzyme for the substrate L-cysteine. M

SUBMITTER: Wang J 

PROVIDER: S-EPMC8466214 | biostudies-literature | 2021 Sep

REPOSITORIES: biostudies-literature