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 bo3.
Keywords:
Cytochrome bd-I; ROS; Redox peptide; Respiratory chain.
Copyright © 2019 Elsevier B.V. and Société Française de Biochimie et Biologie Moléculaire (SFBBM). All rights reserved.
MeSH terms
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Anti-Bacterial Agents / pharmacology*
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Bacteriocins / pharmacology*
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Cyanides / pharmacology
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Cytochrome b Group
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Cytochromes / antagonists & inhibitors
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Cytochromes / genetics
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Cytochromes / metabolism*
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Electron Transport Chain Complex Proteins / antagonists & inhibitors
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Electron Transport Chain Complex Proteins / genetics
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Electron Transport Chain Complex Proteins / metabolism*
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Escherichia coli / drug effects
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Escherichia coli / enzymology*
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Escherichia coli Proteins / antagonists & inhibitors
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Escherichia coli Proteins / genetics
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Escherichia coli Proteins / metabolism*
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Oxidation-Reduction
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Oxidoreductases / antagonists & inhibitors*
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Oxidoreductases / genetics
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Oxidoreductases / metabolism*
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Reactive Oxygen Species / metabolism
Substances
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Anti-Bacterial Agents
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Bacteriocins
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Cyanides
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Cytochrome b Group
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Cytochromes
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Electron Transport Chain Complex Proteins
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Escherichia coli Proteins
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Reactive Oxygen Species
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microcin
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Oxidoreductases
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ubiquinol oxidase
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cytochrome bd terminal oxidase complex, E coli