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InterPro: IPR001457 NADH:ubiquinone/plastoquinone oxidoreductase, chain 6
Protein matches
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UniProtKB Matches: 4764 proteins |
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Accession
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IPR001457 NADH_UbQ/plastoQ_OxRdtase_su6 |
Type
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Family |
Signatures
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GO Term annotation
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Process
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GO:0055114 oxidation reduction
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Function
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GO:0008137 NADH dehydrogenase (ubiquinone) activity
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InterPro annotation
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Entry Details in BioMart
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Abstract
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NADH:ubiquinone oxidoreductase (complex I) (EC:1.6.5.3) 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) [1]. 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 [2], mitochondira, 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 [3]. Mitochondrial complex I, which is located in the inner mitochondrial membrane, is the largest multimeric respiratory enzyme in the mitochondria, consisting of more than 40 subunits, one FMN co-factor and eight FeS clusters [4]. The assembly of mitochondrial complex I is an intricate process that requires the cooperation of the nuclear and mitochondrial genomes [4, 5]. Mitochondrial complex I can cycle between active and deactive forms that can be distinguished by the reactivity towards divalent cations and thiol-reactive agents. All redox prosthetic groups reside in the peripheral arm of the L-shaped structure. The NADH oxidation domain harbouring the FMN cofactor is connected via a chain of iron-sulphur clusters to the ubiquinone reduction site that is located in a large pocket formed by the PSST and 49kDa subunits of complex I [6].
this entry represents chain 6 from NADH:ubiquinone oxidoreductase and NADH-plastoquinone oxidoreductase. Bacterial proton-translocating NADH-quinone oxidoreductase (NDH-1) is composed of 14 different subunits. The chain belonging to this family is a subunit that constitutes the membrane sector of the complex. It reduces ubiquinone to ubiquinol utilising NADH. Plant chloroplastic NADH-plastoquinone oxidoreductase reduces plastoquinone to plastoquinol. Mitochondrial NADH-ubiquinone oxidoreductase from a variety of sources reduces ubiquinone to ubiquinol.
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Database links
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Example proteins
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P03923 NADH-ubiquinone oxidoreductase chain 6
P03925 NADH-ubiquinone oxidoreductase chain 6
P0C329 NAD(P)H-quinone oxidoreductase subunit 6, chloroplastic
P18933 NADH-ubiquinone oxidoreductase chain 6
P60497 NADH-ubiquinone oxidoreductase chain 6
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR001457 |
NADH:ubiquinone/plastoquinone oxidoreductase, chain 6 |
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ModBase |
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Publications
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1.
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Walker JE.
The NADH:ubiquinone oxidoreductase (complex I) of respiratory chains.
Q. Rev. Biophys. 25 253-324 1992
[PubMed: 1470679]
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2.
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Friedrich T, Scheide D.
The respiratory complex I of bacteria, archaea and eukarya and its module common with membrane-bound multisubunit hydrogenases.
FEBS Lett. 479 1-5 2000
[PubMed: 10940377]
http://dx.doi.org/10.1016/S0014-5793(00)01867-6
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3.
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Schneider D, Pohl T, Walter J, Dorner K, Kohlstadt M, Berger A, Spehr V, Friedrich T.
Assembly of the Escherichia coli NADH:ubiquinone oxidoreductase (complex I).
Biochim. Biophys. Acta 1777 735-9 2008
[PubMed: 18394423]
http://dx.doi.org/10.1016/j.bbabio.2008.03.003
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4.
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Remacle C, Barbieri MR, Cardol P, Hamel PP.
Eukaryotic complex I: functional diversity and experimental systems to unravel the assembly process.
Mol. Genet. Genomics 280 93-110 2008
[PubMed: 18563446]
http://dx.doi.org/10.1007/s00438-008-0350-5
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5.
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Vogel RO, Smeitink JA, Nijtmans LG.
Human mitochondrial complex I assembly: a dynamic and versatile process.
Biochim. Biophys. Acta 1767 1215-27 2007
[PubMed: 17854760]
http://dx.doi.org/10.1016/j.bbabio.2007.07.008
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6.
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Zickermann V, Drose S, Tocilescu MA, Zwicker K, Kerscher S, Brandt U.
Challenges in elucidating structure and mechanism of proton pumping NADH:ubiquinone oxidoreductase (complex I).
J. Bioenerg. Biomembr. 40 475-83 2008
[PubMed: 18982432]
http://dx.doi.org/10.1007/s10863-008-9171-9
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InterPro 23.1
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