Gene Symbol: coxIII
Description: Cytochrome c oxidase, aa3-type, subunit III
Species: Rhodobacter sphaeroides 2.4.1

Top Publications

  1. Svensson Ek M, Abramson J, Larsson G, T rnroth S, Brzezinski P, Iwata S. The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides. J Mol Biol. 2002;321:329-39 pubmed
    ..These differences between the structures could reflect conformational changes that take place upon deprotonation of E(I-286) during turnover of the wild-type enzyme, which could be part of the proton-pumping machinery of the enzyme...
  2. Nowak C, Laredo T, Gebert J, Lipkowski J, Gennis R, Ferguson Miller S, et al. 2D-SEIRA spectroscopy to highlight conformational changes of the cytochrome c oxidase induced by direct electron transfer. Metallomics. 2011;3:619-27 pubmed publisher
    ..The activated state was characterized by a higher number of correlated transitions as well as a higher number of amino acids associated with electron transfer...
  3. Alnajjar K, Hosler J, PROCHASKA L. Role of the N-terminus of subunit III in proton uptake in cytochrome c oxidase of Rhodobacter sphaeroides. Biochemistry. 2014;53:496-504 pubmed publisher
    ..Our results indicate that the mutation lowers activity indirectly by slowing the uptake of protons through the D-channel and that the three histidine residues stabilize the interactions between subunit I and subunit III. ..
  4. Alnajjar K, Cvetkov T, PROCHASKA L. Role of phospholipids of subunit III in the regulation of structural rearrangements in cytochrome c oxidase of Rhodobacter sphaeroides. Biochemistry. 2015;54:1053-63 pubmed publisher
    ..In conclusion, these results show that the phospholipids regulate events occurring during electron transfer activity by maintaining the structural integrity of the enzyme at the active site. ..