Chemiosmotic coupling in cytochrome oxidase. Possible protonmotive O loop and O cycle mechanisms.
Using the principle of specific vectorial ligand conduction, we outline directly coupled protonmotive O loop and O cycle mechanisms of cytochrome oxidase action that are analogous to protonmotive Q loop and Q cycle mechanisms of QH2 dehydrogenase action. We discuss these directly coupled mechanisms in the light of available experimental knowledge, and suggest that they may stimulate useful new research initiatives designed to elucidate the osmochemistry of protonmotive oxygen reduction in cytochrome oxidase.
P
P
Mitchell
R
R
Mitchell
A J
AJ
Moody
I C
IC
West
H
H
Baum
J M
JM
Wrigglesworth
D001692:Biological Transport; D055598:Chemical Phenomena; D002621:Chemistry; D003300:Copper / Q000378:metabolism; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000378:metabolism*; D006861:Hydrogen Peroxide / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007473:Ion Channels / Q000378:metabolism; D008564:Membrane Potentials; D009995:Osmosis; D010084:Oxidation-Reduction; D010100:Oxygen; D011522:Protons; D013481:Superoxides / Q000378:metabolism
D007473:Ion Channels; D011522:Protons; D013481:Superoxides; D003300:Copper; D006861:Hydrogen Peroxide; D003576:Electron Transport Complex IV; D010100:Oxygen