High-resolution X-ray structure of Gln143Asn manganese superoxide dismutase captures multiple hydrogen peroxide-binding sites.

ABSTRACT: Human mitochondrial manganese superoxide dismutase (MnSOD) converts superoxide into hydrogen peroxide and molecular oxygen, serving as a key defence against oxidative damage. Despite extensive studies, the full structural characterization of H₂O₂-binding sites in MnSOD remains largely unexplored. Previous H₂O₂-soaked MnSOD structures have identified two distinct H₂O₂-binding sites: one directly ligated to the catalytic manganese (LIG position) and another at the active-site gateway (PEO position) between the second-shell residues Tyr34 and His30. In this study, a kinetically impaired Gln143Asn MnSOD variant is used to trap and explore additional H₂O₂-binding sites beyond the second-shell solvent gate. I

SUBMITTER: Dasgupta M 

PROVIDER: S-EPMC12576686 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature