as outlined in the classic review by Trumpower.53The currently accepted model entails two separateubiquinonereaction centers in subunit III that catalyze theoxidationofubiquinolto reduce two molecules of cytochromec, and hence to O2via C-IV, plus the translocation of four protons from themitochondrial...
(CoQ), to formubiquinol(cyto c). Subsequently, through complex IV (cyto c oxidase), cyto c is accepted by the final acceptor, the oxygen, to produce water. In addition, reduction of electron potential energy leads to mitochondrial matrix protons release into the IMS, setting up a proton-...
CYTOCHROME O UBIQUINOL OXIDASE SUBUNIT FROM GLUCO 专利名称：CYTOCHROME O UBIQUINOL OXIDASE SUBUNIT FROM GLUCONOBACTER OXYDANS 发明人：CHEVREUX, Bastien,MAYER, Anne,Françoise,MEURY, Anja,MOUNCEY, Nigel,John,SHINJOH, Masako 申请号：EP2006001226 申请日：20060210 公开号：WO06/084731P1 公开日：20060817 ...
The purified Escherichia coli cytochrome bo3 ubiquinol oxidase contains four subunits that are each integral components of the cytoplasmic membrane. The molecular weight of each of the subunits has been determined by matrix-assisted laser desorption ionization mass spectrometry (MALDI). The observed molecu...
(2002) Coordination of ubiquinol oxidase and cytochrome cbb(3) oxidase expres- sion by multiple regulators in Rhodobacter capsulatus. J Bacteriol 184: 2815-2820.Swem DL, Bauer CE. 2002. Coordination of ubiquinol oxidase and cytochrome cbb(3) oxidase expression by multiple regulators in Rhodobacter...
protein serine/threonine phosphatase activity protein binding heme binding electron transporter, transferring electrons from CoQH2-cytochrome c reductase complex and cytochrome c oxidase complex activity metal ion binding electron carrier activity iron ion binding lipid binding 参与通路 response to rea...
Cytochrome c oxidase (complex IV, CIV) is known in mammals to exist independently or in association with other respiratory proteins to form supercomplexes (SCs). In Saccharomyces cerevisiae, CIV is found solely in an SC with cytochrome bc1 (complex III,
Subunit CydX of Escherichia coli cytochrome bd ubiquinol oxidase is essential for assembly and stability of the di-heme active site. FEBS Lett. 588, 1537–1541, doi: 10.1016/j.febslet.2014.03.036 (2014). 76. Chen, H., Luo, Q., Yin, J., Gao, T. & Gao, H. Evidence for the ...
Homology in the structure and the prosthetic groups between two different terminal ubiquinol oxidases, cytochrome α1 and cytochrome o, of Acetobacter aceti Adachi, Homology in the structure and the prosthetic groups between two different terminal ubiquinol oxidases, cytochrome a1 and cytochrome o, ...
Tsukihara and collaborators resolved the crystal structure of the metal sites and the whole complex with the 13 subunits of the bovine heart cytochrome oxidase at 2.8 Å resolution. Both heme a and the binuclear center a3-CuB are located in COX1 (subunit 1) whereas the binuclear CuA center...