NADH-quinone oxidoreductase

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Function

NADH-quinone oxidoreductase (NQO) (Complex I) pumps protons across the membrane of mitochondria or plasma in bacteria. NQO contains 14 central subunits and up to 32 accessory subunits. NQO contains FMN and 8 to 9 iron-sulfur clusters. Seven of the iron-sulfur clusters form a linear electron transfer chain between the FMN and quinone[1].

For more details see NADH:ubiquinone oxidoreductase

NADH quinone oxidoreductase (NQO1) with inhibitor dicoumarol.


NADH-quinone oxidoreductase chains 1 (grey), 2 (green), 3 (pink), 4 (yellow), 5 (magenta), 6 (cyan), 9 (gold), 15 (red) + Fe4S4 + Fe2S2 + FMN (PDB ode 3i9v).

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NADH-quinone oxidoreductase 3D structures

3D Structures of NADH-quinone oxidoreductase

Updated on 16-November-2021

4hea, 3m9s, 3ias, 3i9v, 6y11 – TtNQO complex I - Thermus thermophilus
6zjl, 6zjn, 6zjy – TtNQO complex I – Cryo EM
2fug – TtNQO complex I + conserved protein
3iam – TtNQO complex I + NADH
6ziy – TtNQO complex I + NADH – Cryo EM
2ybb – TtNQO complex I + cytochrome B,C1 + cytochrome C oxidase – Cryo-EM
6i0d – TtNQO complex I + decyl-ubiquinone
6i1p – TtNQO complex I + NADH
6q8o, 6q8w – TtNQO complex I + antibiotic
6q8x – TtNQO complex I + insecticide
5b3p, 5b3q – TtNQO chain 5
4he8 – TtNQO chains 7,8,10,11,12,13,14 membrane domain
3m9c, 3rko – NQO subunits NUOA,J,K,L,M,N membrane domain – Escherichia coli
3lwx – NQO subunit C – Parabacteroides distasonis
6q9c, 6hl3, 6hl2 – AaNQO subunits E,F + Fe4S4 + Fe2S2 + FMN + NADH – Aquifex aeolicus
6q9g, 6q9j, 6q9k, 6r7p, 6hlm, 6hlj, 6hli, 6hla, 6hl4 – AaNQO subunits E (mutant),F + Fe4S4 + Fe2S2 + FMN + NADH
6saq – AaNQO subunits E,F + Fe4S4 + Fe2S2 + FMN + inhibitor
6nby, 6nbx, 6nbq, 6hum, 6khj, 6l7p – TeNQO complex I + TLR0636 – Thermosynechococcus elongatus – Cryo-EM
6khi, 6l7o – TeNQO complex I + ferredoxin + TLR0636 + TLR0472 – Cryo EM
6tjv – TeNQO complex I + ferredoxin + TLR0636 + TLR0906 + TLR0220 – Cryo EM

References

  1. Brandt U. Energy converting NADH:quinone oxidoreductase (complex I). Annu Rev Biochem. 2006;75:69-92. PMID:16756485 doi:http://dx.doi.org/10.1146/annurev.biochem.75.103004.142539

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Michal Harel

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