NADH_4Fe-4SNADH-ubiquinone oxidoreductase-F iron-sulfur binding region
|SMART accession number:||SM00928|
|Interpro abstract (IPR019575):|
NADH:ubiquinone oxidoreductase (complex I) (EC 220.127.116.11) 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) [(PUBMED:1470679)]. 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 [(PUBMED:10940377)], 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 [(PUBMED:18394423)].
This entry describes the F subunit of complexes that resemble NADH-quinone oxidoreductases. The electron acceptor is a quinone, ubiquinone, in mitochondria and most bacteria, including Escherichia coli, where the recommended gene symbol is nuoF. This family does not have any members in chloroplast or cyanobacteria, where the quinone may be plastoquinone and NADH may be replaced by NADPH, nor in Methanosarcina, where NADH is replaced by F420H2.
This entry represents the iron-sulphur binding domain of the F subunit.
|GO process:||oxidation-reduction process (GO:0055114)|
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