Lactoperoxidase catalytically oxidize hydrogen sulfide via intermediate formation of sulfheme derivatives.

ABSTRACT: The biological chemistry of hydrogen sulfide (H₂S) with physiologically important heme proteins is in the focus of redox biology research. In this study, we investigated the interactions of lactoperoxidase (LPO) with H₂S in the presence and absence of molecular dioxygen (O₂) or hydrogen peroxide (H₂O₂). Under anaerobic conditions, native LPO forms no heme-H₂S complex upon sulfide exposure. However, under aerobic conditions or in the presence of H₂O₂ the formation of both ferrous and ferric sulfheme (sulfLPO) derivatives was observed based on the appearances of their characteristic optical absorptions at 638 nm and 727 nm, respectively. Interestingly, we demonstrate that LPO can catalytically oxidize H

SUBMITTER: Rios-Gonzalez BB 

PROVIDER: S-EPMC11238738 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature