Redox Processes Controlling the Biogenesis of c-Type Cytochromes

被引：27

作者：

Bonnard, Geraldine ^{[1
]}

Corvest, Vincent ^{[2
,3
]}

Meyer, Etienne H. ^{[1
]}

Hamel, Patrice P. ^{[2
,3
]}

机构：

[1] Univ Strasbourg, CNRS, UPR2357, Inst Biol Mol Plantes, F-67084 Strasbourg, France

[2] Ohio State Univ, Dept Mol Genet, Columbus, OH 43210 USA

[3] Ohio State Univ, Dept Mol & Cellular Biochem, Columbus, OH 43210 USA

来源：

ANTIOXIDANTS & REDOX SIGNALING | 2010年 / 13卷 / 09期

基金：

美国国家科学基金会;

关键词：

HEME CHAPERONE CCME; MITOCHONDRIAL INTERMEMBRANE SPACE; THIOL-DISULFIDE OXIDOREDUCTASES; MATURATION PROTEIN CCME; BACILLUS-SUBTILIS RESA; ESCHERICHIA-COLI CCMG; APOCYTOCHROME-C; IN-VITRO; BOND FORMATION; BINDING SITE;

D O I：

10.1089/ars.2010.3161

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：

In mitochondria, two mono heme c-type cytochromes are essential electron shuttles of the respiratory chain. They are characterized by the covalent attachment of their heme C to a CXXCH motif in the apoproteins. This post-translational modification occurs in the intermembrane space compartment. Dedicated assembly pathways have evolved to achieve this chemical reaction that requires a strict reducing environment. In mitochondria, two unrelated machineries operate, the rather simple System III in yeast and animals and System I in plants and some protozoans. System I is also found in bacteria and shares some common features with System II that operates in bacteria and plastids. This review aims at presenting how different systems control the chemical requirements for the heme ligation in the compartments where cytochrome c maturation takes place. A special emphasis will be given on the redox processes that are required for the heme attachment reaction onto apocytochromes c. Antioxid. Redox Signal. 13, 1385-1401.

引用

页码：1385 / 1401

页数：17

共 106 条

[1] Helix swapping leads to dimerization of the N-terminal domain of the c-type cytochrome maturation protein CcmH from Escherichia coli [J].