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

被引：14
作者：
Emilce Galvan, Adriana [1 ,2 ]
Carolina Chalon, Miriam [1 ,2 ]
Rios Colombo, Natalia Soledad [1 ,2 ]
Schurig-Briccio, Lici Ariane [3 ]
Sosa-Padilla, Bernardo [4 ]
Gennis, Robert B. [3 ]
Bellomio, Augusto [1 ,2 ]
机构：
[1] Univ Nacl Tucuman, Fac Bioquim Quim & Farm, CONICET UNT, Inst Super Invest Biol INSIBIO, Chacabuco 461, San Miguel De Tucuman, Tucuman, Argentina
[2] Univ Nacl Tucuman, Fac Bioquim Quim & Farm, Inst Quim Biol Dr Bernabe Bloj, Chacabuco 461, San Miguel De Tucuman, Tucuman, Argentina
[3] Univ Illinois, Dept Biochem, Urbana, IL 61801 USA
[4] PROIMI CONICET, Planta Piloto Proc Ind Microbiol, Ave Belgrano & Pasaje Caseros,T4001MVB, San Miguel De Tucuman, Tucuman, Argentina
来源：
BIOCHIMIE | 2019年 / 160卷
关键词：
Redox peptide; Cytochrome bd-I; Respiratory chain; ROS; FAST INTERACTION REFINEMENT; ANTIMICROBIAL PEPTIDE; RNA-POLYMERASE; SUPEROXIDE; MECHANISMS; EXPRESSION; FIREDOCK; COMPLEX; BINDING; PROTEIN;
D O I：
10.1016/j.biochi.2019.02.007
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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). (C) 2019 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.
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收藏
页码：141 / 147
页数：7
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