|1nek, resolution 2.60Å ()|
|Ligands:||, , , , , , , , ,|
|Gene:||SDHA OR B0723 OR Z0877 OR ECS0748 (Escherichia coli), SDHB OR B0724 (Escherichia coli), SDHC OR CYBA OR B0721 OR Z0875 OR ECS0746 (Escherichia coli), SDHD OR B0722 (Escherichia coli)|
Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound
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.
Architecture of succinate dehydrogenase and reactive oxygen species generation., Yankovskaya V, Horsefield R, Tornroth S, Luna-Chavez C, Miyoshi H, Leger C, Byrne B, Cecchini G, Iwata S, Science. 2003 Jan 31;299(5607):700-4. PMID:12560550
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
- 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. PMID:12560550 doi:10.1126/science.1079605
- Rothery EL, Mowat CG, Miles CS, Mott S, Walkinshaw MD, Reid GA, Chapman SK. Probing domain mobility in a flavocytochrome. Biochemistry. 2004 May 4;43(17):4983-9. PMID:15109257 doi:10.1021/bi030261w