An Electron-Transfer Path through an Extended Disulfide Relay System: The Case of the Redox Protein ALR

被引:36
作者
Banci, Lucia [1 ,2 ]
Bertini, Ivano [1 ,2 ]
Calderone, Vito [1 ,2 ]
Cefaro, Chiara [1 ,2 ]
Ciofi-Baffoni, Simone [1 ,2 ]
Gallo, Angelo [1 ,2 ]
Tokatlidis, Kostas [3 ,4 ]
机构
[1] Univ Florence, Magnet Resonance Ctr, Sesto Fiorentino, Italy
[2] Univ Florence, Dept Chem, Sesto Fiorentino, Italy
[3] Fdn Res & Technol Hellas, Inst Mol Biol & Biotechnol, Iraklion 70013, Crete, Greece
[4] Univ Crete, Dept Mat Sci & Technol, Iraklion 71003, Crete, Greece
关键词
MITOCHONDRIAL INTERMEMBRANE SPACE; DEPENDENT SULFHYDRYL OXIDASES; LIVER-REGENERATION; BOND FORMATION; EGG-WHITE; FLAVIN; MIA40; SUBSTRATE; AUGMENTOR; IMPORT;
D O I
10.1021/ja209881f
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The oxidative folding mechanism in the intermembrane space of human mitochondria underpins a disulfide relay system consisting of the import receptor Mia40 and the homodimeric FAD-dependent thiol oxidase ALR. The flavoprotein ALR receives two electrons per subunit from Mia40, which are then donated through one-electron reactions to two cytochrome c molecules, thus mediating a switch from two-electron to one-electron transfer. We dissect here the mechanism of the electron flux within ALR, characterizing at the atomic level the ALR intermediates that allow electrons to rapidly flow to cytochrome c. The intermediate critical for the electron-transfer process implies the formation of a specific inter-subunit disulfide which exclusively allows electron flow from Mia40 to FAD. This finding allows us to present a complete model for the electron-transfer pathway in ALR
引用
收藏
页码:1442 / 1445
页数:4
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