Quantitative mapping of methionine sensitivity to oxidation in the copper-bound PcuC chaperone.

ABSTRACT: Copper is typically coordinated by histidine, cysteine, or methionine in proteins, and these residues are particularly sensitive to oxidation. However, it remains unclear whether copper-coordinating residues are more prone to oxidation than non-coordinating ones, and how their susceptibility changes between the apo and copper-bound states. The copper chaperone PcuC, important for cytochrome c oxidase assembly in bacteria, contains a canonical binding site composed of two histidines and two methionines (H51x_nM63 × ₂₂H86xM88), as well as a disordered C-terminal extension enriched in methionine and histidine. To quantify methionine oxidation sensitivity in both apo- and Cu-bound PcuC, we used a methionine-specific oxaziridine probe combined with mass spectrometry and com

SUBMITTER: Tarrago L 

PROVIDER: S-EPMC12860648 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature