Strategy of research on the chemiosmotic mechanism of cytochrome oxidase.
In recent papers on protonmotive redox mechanisms in cytochrome oxidase in [(1987) FEBS Lett. 222, 235-245] and [Glynn Biological Research Reports (1987) 3, 1-7], I have suggested that a copper centre may enable the H2O/OH or H2O/O couple to act as the hydrogen-carrying arm of a redox loop by means of a (CuOH2)+/(CuOH)+ or (CuOH2)+/(CuO)+ system at the centre. I here explain that critical comments by Malmström [(1988) FEBS Lett. 231, 268-269] on the first of these papers, which might also be levelled at the second, depend on a misunderstanding. I also respond to Malmström's comment about testing conformationally coupled proton-pump mechanisms.
Mitchell
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Glynn Research Institute, Bodmin, Cornwall, England.
D003576:Electron Transport Complex IV / Q000378:metabolism*; D010084:Oxidation-Reduction; D011522:Protons; D012107:Research Design
D011522:Protons; D003576:Electron Transport Complex IV