title: Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans.
abstract: The crystal structure at 2.8 A resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with antibody Fv fragment, is described. Subunit I contains 12 membrane-spanning, primarily helical segments and binds haem a and the haem a3-copper B binuclear centre where molecular oxygen is reduced to water. Two proton transfer pathways, one for protons consumed in water formation and one for 'proton pumping', could be identified. Mechanisms for proton pumping are discussed.
authors.affiliation: Max-Planck-Institut für Biophysik, Frankfurt/M., Germany.
authors.forename: S
authors.initials: S
authors.lastname: Iwata
authors.forename: C
authors.initials: C
authors.lastname: Ostermeier
authors.forename: B
authors.initials: B
authors.lastname: Ludwig
authors.forename: H
authors.initials: H
authors.lastname: Michel
mesh_terms: D003196:Computer Graphics; D003300:Copper / Q000737:chemistry; D018360:Crystallography, X-Ray; D003576:Electron Transport Complex IV / Q000737:chemistry*; D006418:Heme / Q000031:analogs & derivatives / Q000737:chemistry; D010231:Paracoccus denitrificans / Q000201:enzymology*; D011485:Protein Binding; D011487:Protein Conformation; D017494:Proton Pumps
chemical_list: D017494:Proton Pumps; C027728:heme a; D006418:Heme; D003300:Copper; D003576:Electron Transport Complex IV