NADH-quinone oxidoreductase

From Proteopedia

spinqualitylabelsall models 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). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image 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.

3D Structures of NADH-quinone oxidoreductase

Updated on 05-November-2019

2fug – TtNQO chains 1,2,3,4,5,6,9 + conserved protein + Fe4S4 + Fe2S2 + FMN – Thermus thermophilus
5b3p, 5b3q – TtNQO chain 5
3i9v – TtNQO chains 1,2,3,4,5,6,9,15 + Fe4S4 + Fe2S2 + FMN
3iam – TtNQO chains 1,2,3,4,5,6,9,15 + Fe4S4 + Fe2S2 + FMN + NADH
3ias – TtNQO chains 1,2,3,4,5,6,9,15 + Fe4S4 + Fe2S2 + FMN
3m9s – TtNQO chains 1,2,3,4,7,8,10,11,12,13,14,15,B,C,I,15 + Fe4S4 + Fe2S2 + FMN
4hea – TtNQO chains 1,2,3,4,5,6,7,8,9,10,11,12,13,14,15 + Fe4S4 + Fe2S2 + FMN
4he8 – TtNQO chains 7,8,10,11,12,13,14 membrane domain
2ybb – TtNQO chains 1,2,3,4,5,6,9,15,M,N,K + cytochrome B,C1 + cytochrome C oxidase + Fe4S4 + Fe2S2 + FMN – Cryo-EM
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
6nby, 6nbx, 6nbq, 6hum – NQO chains 1,2,3,4,4L,5,I,J,H,K,L,M,N,O,P,Q + Fe4S4 + TLR0636 – Thermosynechococcus elongatus – 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