| Structural highlights
6rko is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| | Ligands: | HDD, HEB, OXY, POV, UQ8 |
| Activity: | Ubiquinol oxidase (electrogenic, proton-motive force generating), with EC number 7.1.1.7 |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[CYDX_ECOLI] Required for correct functioning of cytochrome bd-I oxidase. This protein and AppX may have some functional overlap. [CYDB_ECOLI] A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.[1] [2] [3] [CYDA_ECOLI] A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron.[4] [5] [6] [7] [8]
References
- ↑ Bekker M, de Vries S, Ter Beek A, Hellingwerf KJ, de Mattos MJ. Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase. J Bacteriol. 2009 Sep;191(17):5510-7. doi: 10.1128/JB.00562-09. Epub 2009 Jun 19. PMID:19542282 doi:https://dx.doi.org/10.1128/JB.00562-09
- ↑ Borisov VB, Murali R, Verkhovskaya ML, Bloch DA, Han H, Gennis RB, Verkhovsky MI. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc Natl Acad Sci U S A. 2011 Oct 18;108(42):17320-4. doi:, 10.1073/pnas.1108217108. Epub 2011 Oct 10. PMID:21987791 doi:https://dx.doi.org/10.1073/pnas.1108217108
- ↑ Miller MJ, Gennis RB. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol Chem. 1983 Aug 10;258(15):9159-65. PMID:6307994
- ↑ Bekker M, de Vries S, Ter Beek A, Hellingwerf KJ, de Mattos MJ. Respiration of Escherichia coli can be fully uncoupled via the nonelectrogenic terminal cytochrome bd-II oxidase. J Bacteriol. 2009 Sep;191(17):5510-7. doi: 10.1128/JB.00562-09. Epub 2009 Jun 19. PMID:19542282 doi:https://dx.doi.org/10.1128/JB.00562-09
- ↑ Borisov VB, Murali R, Verkhovskaya ML, Bloch DA, Han H, Gennis RB, Verkhovsky MI. Aerobic respiratory chain of Escherichia coli is not allowed to work in fully uncoupled mode. Proc Natl Acad Sci U S A. 2011 Oct 18;108(42):17320-4. doi:, 10.1073/pnas.1108217108. Epub 2011 Oct 10. PMID:21987791 doi:https://dx.doi.org/10.1073/pnas.1108217108
- ↑ Fang H, Lin RJ, Gennis RB. Location of heme axial ligands in the cytochrome d terminal oxidase complex of Escherichia coli determined by site-directed mutagenesis. J Biol Chem. 1989 May 15;264(14):8026-32. PMID:2656671
- ↑ Miller MJ, Gennis RB. The purification and characterization of the cytochrome d terminal oxidase complex of the Escherichia coli aerobic respiratory chain. J Biol Chem. 1983 Aug 10;258(15):9159-65. PMID:6307994
- ↑ Kaysser TM, Ghaim JB, Georgiou C, Gennis RB. Methionine-393 is an axial ligand of the heme b558 component of the cytochrome bd ubiquinol oxidase from Escherichia coli. Biochemistry. 1995 Oct 17;34(41):13491-501. doi: 10.1021/bi00041a029. PMID:7577938 doi:https://dx.doi.org/10.1021/bi00041a029
|
