Is a third proton-conducting pathway operative in bacterial cytochrome c oxidase?
Despite the existence of several three-dimensional structures of cytochrome c oxidases, a detailed understanding of pathways involved in proton movements through the complex remains largely elusive. Next to the two well-established pathways (termed D and K), an additional proton-conducting network ('H-channel') has been proposed for the beef heart enzyme. Yet, our recent mutational studies on corresponding residues of the Paracoccus denitrificans cytochrome c oxidase provide no clues that such a pathway operates in the prokaryotic enzyme.
Salje
J
J
Molecular Genetics Group, Institute for Biochemistry, Johann Wolfgang Goethe Universität, Biozentrum, Marie-Curie-Strasse 9, D-60439 Frankfurt/M, Germany.
Ludwig
B
B
Richter
O-M H
OM
D001426:Bacterial Proteins / Q000378:metabolism*; D001692:Biological Transport; D003576:Electron Transport Complex IV / Q000378:metabolism*; D006859:Hydrogen / Q000378:metabolism; D007473:Ion Channels / Q000378:metabolism; D011522:Protons; D011549:Pseudomonas / Q000201:enzymology
D001426:Bacterial Proteins; D007473:Ion Channels; D011522:Protons; D006859:Hydrogen; D003576:Electron Transport Complex IV