1nek

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Complex II (Succinate Dehydrogenase) From E. Coli with ubiquinone bound

Overview

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.

About this Structure

1NEK is a Protein complex structure of sequences from Escherichia coli with OAA, CA, FAD, FES, SF4, F3S, HEM, UQ2, CDN and EPH as ligands. Full crystallographic information is available from OCA.

Reference

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

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