Architecture of succinate dehydrogenase and reactive oxygen species generation.

Article Details

Citation

Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S

Architecture of succinate dehydrogenase and reactive oxygen species generation.

Science. 2003 Jan 31;299(5607):700-4.

PubMed ID
12560550 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Succinate dehydrogenase flavoprotein subunitP0AC41Details
Succinate dehydrogenase iron-sulfur subunitP07014Details
Succinate dehydrogenase cytochrome b556 subunitP69054Details
Succinate dehydrogenase hydrophobic membrane anchor subunitP0AC44Details