Architecture of succinate dehydrogenase and reactive oxygen species generation

被引：729

作者：

Yankovskaya, V

Horsefield, R

Törnroth, S

Luna-Chavez, C

Miyoshi, H

Léger, C

Byrne, B

Cecchini, G ^{[1
]}

Iwata, S

机构：

[1] Univ London Imperial Coll Sci Technol & Med, Dept Biol Sci, London SW7 2AY, England

[2] Vet Adm Med Ctr, Div Mol Biol, San Francisco, CA 94121 USA

[3] Uppsala Univ, Dept Biochem, S-75123 Uppsala, Sweden

[4] Univ Calif San Francisco, Dept Biochem & Biophys, San Francisco, CA 94143 USA

[5] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Sakyo Ku, Kyoto 6068502, Japan

[6] Univ Oxford, Inorgan Chem Lab, Oxford OX1 3QR, England

[7] Univ London Imperial Coll Sci Technol & Med, Div Biomed Sci, London SW7 2AZ, England

来源：

SCIENCE | 2003年 / 299卷 / 5607期

关键词：

D O I：

10.1126/science.1079605

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The structure of Escherichia coli succinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron donor, succinate, to the terminal electron acceptor, ubiquinone. It was found that the SQR redox centers are arranged in a manner that aids the prevention of reactive oxygen species (ROS) formation at the flavin adenine dinucleotide. This is likely to be the main reason SQR is expressed during aerobic respiration rather than the related enzyme fumarate reductase, which produces high levels of ROS. Furthermore, symptoms of genetic disorders associated with mitochondrial SQR mutations may be a result of ROS formation resulting from impaired electron transport in the enzyme.

引用

页码：700 / 704

页数：5

共 31 条

[1] INTERACTIONS OF OXALOACETATE WITH ESCHERICHIA-COLI FUMARATE REDUCTASE [J].