sodC1

sodC1 is a bacterial gene that encodes a periplasmic copper/zinc superoxide dismutase (CuZn-SOD). In species that possess multiple sodC genes, the paralogs are often designated sodC1 and sodC2, with sodC1 representing the first identified copy. These enzymes form part of the organism’s defense against reactive oxygen species and are distinct from cytosolic superoxide dismutases encoded by sodA or sodB.

The encoded enzyme detoxifies superoxide radicals by catalyzing their conversion to molecular oxygen and hydrogen peroxide within the periplasm. Its periplasmic localization is achieved by an N-terminal signal peptide that directs the protein to the Sec secretion pathway and is typically removed after export. The mature enzyme usually functions as a dimer and requires copper and zinc as cofactors for catalytic activity.

Biochemical and structural characteristics place SodC1 in the CuZn-SOD family, with the active site containing histidine ligands that coordinate the metal ions. This configuration enables rapid dismutation of superoxide and contributes to protection of periplasmic components from oxidative damage.

Regulation and biological significance of sodC1 can vary by species but often involves responses to oxidative stress. Expression of sodC1 may be triggered by exposure to reactive oxygen species and can contribute to survival in environments where the bacterial cell encounters host defenses or environmental oxidants. In some pathogenic bacteria, periplasmic SodC1 activity is associated with increased resistance to host-derived oxidative bursts and can influence virulence traits.

Overall, sodC1 represents a conserved component of the bacterial oxidative stress response, encoding a periplasmic CuZn-SOD that complements cytosolic SODs in maintaining redox homeostasis.