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

Adriana Emilce Galván, Miriam Carolina Chalón, Natalia Soledad Ríos Colombo, Lici Ariane Schurig-Briccio, Bernardo Sosa-Padilla, Robert B. Gennis, Augusto Bellomio

Research output: Contribution to journalArticle

Abstract

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 .

Original languageEnglish (US)
Pages (from-to)141-147
Number of pages7
JournalBiochimie
Volume160
DOIs
StatePublished - May 2019

Keywords

  • Cytochrome bd-I
  • ROS
  • Redox peptide
  • Respiratory chain

ASJC Scopus subject areas

  • Biochemistry

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    Galván, A. E., Chalón, M. C., Ríos Colombo, N. S., Schurig-Briccio, L. A., Sosa-Padilla, B., Gennis, R. B., & Bellomio, A. (2019). Microcin J25 inhibits ubiquinol oxidase activity of purified cytochrome bd-I from Escherichia coli. Biochimie, 160, 141-147. https://doi.org/10.1016/j.biochi.2019.02.007