BIOMAT Database Logo BIOMAT Database Logo

Microcin J25 inhibits ubiquinol oxidase activity of purified cytochrome bd-I from Escherichia coli. 2019

Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
Instituto Superior de Investigaciones Biológicas (INSIBIO, CONICET-UNT) e Instituto de Química Biológica "Dr. Bernabé Bloj", Facultad de Bioquímica, Química y Farmacia, Universidad Nacional de Tucumán, Chacabuco 461, San Miguel de Tucumán, Argentina.

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.

UI MeSH Term Description Entries
D010084 Oxidation-Reduction A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471). Redox,Oxidation Reduction
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D003486 Cyanides Inorganic salts of HYDROGEN CYANIDE containing the -CN radical. The concept also includes isocyanides. It is distinguished from NITRILES, which denotes organic compounds containing the -CN radical. Cyanide,Isocyanide,Isocyanides
D003573 Cytochrome b Group Cytochromes (electron-transporting proteins) with protoheme (HEME B) as the prosthetic group. Cytochromes Type b,Cytochromes, Heme b,Group, Cytochrome b,Heme b Cytochromes,Type b, Cytochromes,b Cytochromes, Heme,b Group, Cytochrome
D003580 Cytochromes Hemeproteins whose characteristic mode of action involves transfer of reducing equivalents which are associated with a reversible change in oxidation state of the prosthetic group. Formally, this redox change involves a single-electron, reversible equilibrium between the Fe(II) and Fe(III) states of the central iron atom (From Enzyme Nomenclature, 1992, p539). The various cytochrome subclasses are organized by the type of HEME and by the wavelength range of their reduced alpha-absorption bands. Cytochrome
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000900 Anti-Bacterial Agents Substances that inhibit the growth or reproduction of BACTERIA. Anti-Bacterial Agent,Anti-Bacterial Compound,Anti-Mycobacterial Agent,Antibacterial Agent,Antibiotics,Antimycobacterial Agent,Bacteriocidal Agent,Bacteriocide,Anti-Bacterial Compounds,Anti-Mycobacterial Agents,Antibacterial Agents,Antibiotic,Antimycobacterial Agents,Bacteriocidal Agents,Bacteriocides,Agent, Anti-Bacterial,Agent, Anti-Mycobacterial,Agent, Antibacterial,Agent, Antimycobacterial,Agent, Bacteriocidal,Agents, Anti-Bacterial,Agents, Anti-Mycobacterial,Agents, Antibacterial,Agents, Antimycobacterial,Agents, Bacteriocidal,Anti Bacterial Agent,Anti Bacterial Agents,Anti Bacterial Compound,Anti Bacterial Compounds,Anti Mycobacterial Agent,Anti Mycobacterial Agents,Compound, Anti-Bacterial,Compounds, Anti-Bacterial
D001430 Bacteriocins Substances elaborated by specific strains of bacteria that are lethal against other strains of the same or related species. They are protein or lipopolysaccharide-protein complexes used in taxonomy studies of bacteria. Bacteriocin,Lantibiotic,Lantibiotics
D017382 Reactive Oxygen Species Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of SIGNAL TRANSDUCTION and GENE EXPRESSION, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS. Active Oxygen Species,Oxygen Radical,Oxygen Radicals,Pro-Oxidant,Reactive Oxygen Intermediates,Active Oxygen,Oxygen Species, Reactive,Pro-Oxidants,Oxygen, Active,Pro Oxidant,Pro Oxidants,Radical, Oxygen
D045222 Electron Transport Chain Complex Proteins A complex of enzymes and PROTON PUMPS located on the inner membrane of the MITOCHONDRIA and in bacterial membranes. The protein complex provides energy in the form of an electrochemical gradient, which may be used by either MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES or BACTERIAL PROTON-TRANSLOCATING ATPASES.

Related Publications

Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
Identification of a stable semiquinone intermediate in the purified and membrane bound ubiquinol oxidase-cytochrome bd from Escherichia coli.
July 1998, European journal of biochemistry,
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
Cyanide-binding site of bd-type ubiquinol oxidase from Escherichia coli.
December 1995, The Journal of biological chemistry,
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
Electron transfer process in cytochrome bd-type ubiquinol oxidase from Escherichia coli revealed by pulse radiolysis.
May 1999, Biochemistry,
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
Antibacterial activity evaluation of microcin J25 against diarrheagenic Escherichia coli.
October 2000, Applied and environmental microbiology,
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
Spectroscopic evidence for a heme-heme binuclear center in the cytochrome bd ubiquinol oxidase from Escherichia coli.
June 1993, Proceedings of the National Academy of Sciences of the United States of America,
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli.
April 1996, The Journal of biological chemistry,
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
In Escherichia coli Ammonia Inhibits Cytochrome bo3 But Activates Cytochrome bd-I.
December 2020, Antioxidants (Basel, Switzerland),
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
Peroxidase activity of cytochrome bd from Escherichia coli.
April 2010, Biochemistry. Biokhimiia,
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
The orientation of the three haems of the 'in situ' ubiquinol oxidase, cytochrome bd, of Escherichia coli.
February 1992, The Biochemical journal,
Adriana Emilce Galván, and Miriam Carolina Chalón, and Natalia Soledad Ríos Colombo, and Lici Ariane Schurig-Briccio, and Bernardo Sosa-Padilla, and Robert B Gennis, and Augusto Bellomio
Mass spectrometric analysis of the ubiquinol-binding site in cytochrome bd from Escherichia coli.
January 2006, The Journal of biological chemistry,
Copied contents to your clipboard!