Microcin J25 inhibits ubiquinol oxidase activity of purified cytochrome bd-I from Escherichia coli

CHALÓN, MIRIAM CAROLINA; SOSA-PADILLA, BERNARDO; RÍOS COLOMBO, NATALIA SOLEDAD; GENNIS, ROBERT B; GALVÁN, ADRIANA EMILCE; SCHURIG-BRICCIO, LICI ARIANE; BELLOMIO, AUGUSTO

BIOCHIMIE

ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER

Año: 2019 vol. 160 p. 141 - 147

0300-9084

Microcin J25 (MccJ25), an antimicrobial peptide, targets the respiratory chain but the exact mechanism by which it does so remains unclear. Here, we reveal that MccJ25 is able to inhibit the enzymatic activity of the isolated cytochrome bd-I from E. coli and induces at the same time production of reactive oxygen species. MccJ25 behaves as a dose-dependent weak inhibitor. Intriguingly, MccJ25 is capable of producing a change in the oxidation state of cytochrome bd-I causing its partial reduction in the presence of cyanide. These effects are specific for cytochrome bd-I, since the peptide is not able to act on purified cytochrome bo 3 .