| Description | NADH:ubiquinone oxidoreductase (complex I) ( ) is a respiratory-chain enzyme that catalyses the transfer of two electrons from NADH to ubiquinone in a reaction that is associated with proton translocation across the membrane (NADH + ubiquinone = NAD+ + ubiquinol) [ ]. Complex I is a major source of reactive oxygen species (ROS) that are predominantly formed by electron transfer from FMNH(2). Complex I is found in bacteria, cyanobacteria (as a NADH-plastoquinone oxidoreductase), archaea [], mitochondria, and in the hydrogenosome, a mitochondria-derived organelle. In general, the bacterial complex consists of 14 different subunits, while the mitochondrial complex contains homologues to these subunits in addition to approximately 31 additional proteins [].This entry represents the Na(+)-translocating E subunit from NADH:ubiquinone oxidoreductase. NADH can be oxidized by the respiratory chain of bacteria via NADH:quinone oxidoreductases that belong to three distinct enzyme families: NDH-1, NDH-2, and NQR. The NQR-type enzymes are sodium-motive NADH:quinone oxidoreductases consisting of six subunits (NqrA-F) and several cofactors: FAD, 2 FMN, a 2Fe-2S cluster and riboflavin. The NADH:quinone oxidoreductase activity of these enzymes is stimulated by sodium ions and is coupled with pumping of Na+ but not H+. Subunits NqrA, NqrC and NqrF represent the three major subunits of the NQR complex, which are alpha, gamma and beta, respectively. Subunits NqrB, NqrD and NqrE are very hydrophobic polypeptides that were found to co-localise with the alpha subunit [ ]. | Name | Na(+)-translocating NADH-quinone reductase subunit E |
| Short Name | NqrE | Type | Family |
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