A new redox loop formality involving metal-catalysed hydroxide-ion translocation. A hypothetical Cu loop mechanism for cytochrome oxidase.
A new hypothetical type of redox loop is described, which translocates hydroxide instead of protons. Conventional protonmotive redox loops use carriers of protons with electrons (e.g. QH2/Q systems) to couple electron transfer to the translocation of protons. The putative hydroxidemotive redox loop uses carriers of hydroxide ions against electrons (e.g. transition-metal centres) to couple electron transfer to the translocation of hydroxide ions. This simple idea leads to the proposal of a hydroxidemotive Cu loop mechanism that may possibly be applicable to the CuA or CuB centre of cytochrome oxidase, and might thus account for the coupling of electron transfer to net proton translocation in that osmoenzyme.
Mitchell
P
P
Glynn Research Institute, Bodmin, England.
D003300:Copper / Q000494:pharmacology*; D004579:Electron Transport; D003576:Electron Transport Complex IV / Q000378:metabolism*; D006878:Hydroxides; D010084:Oxidation-Reduction
D006878:Hydroxides; D003300:Copper; D003576:Electron Transport Complex IV