The oxidized subunit B8 from human complex I adopts a thioredoxin fold

被引：23

作者：

Brockmann, C

Diehl, A

Rehbein, K

Strauss, H

Schmieder, P

Korn, B

Kühne, R

Oschkinat, H ^{[1
]}

机构：

[1] Forschungsinst Mol Pharmakol, D-13125 Berlin, Germany

[2] Free Univ Berlin, Fac Biol Chem & Pharm, D-14195 Berlin, Germany

[3] Deutsch Ressourcenzentrum Genomforsch, D-65120 Heidelberg, Germany

来源：

STRUCTURE | 2004年 / 12卷 / 09期

关键词：

D O I：

10.1016/j.str.2004.06.021

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：

Subunit B8 from ubiquinone oxidoreductase (complex I) (CI-B8) is one of several nuclear-encoded supernumerary subunits that are not present in bacterial complex I. Its solution structure shows a thioredoxin fold with highest similarities to the human thioredoxin mutant C73S and thioredoxin 2 from Anabeana sp. Interestingly, these proteins contain active sites in the same area, where the disulfide bond of oxidized CI-B8 is located. The redox potential of this disulfide bond is -251.6 mV, comparing well to that of disulfides in other thioredoxin-like proteins. Analysis of the structure reveals a surface area that is exclusively composed of highly conserved residues and thus most likely a subunit interaction site within complex I.

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页码：1645 / 1654

页数：10

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