Characterization of the intermediates in the reaction of membrane-bound mixed-valence-state cytochrome oxidase with oxygen at low temperatures by optical spectroscopy in the visible region.
The 'pure' difference spectra of the three species, IM, IIM and IIIM, formed in the low-temperature reaction of membrane-bound mixed-valence-state cytochrome oxidase with O2 relative to unliganded membrane-bound mixed-valence-state cytochrome oxidase were characterized by optical spectroscopy in the visible region. The difference spectrum of species IM was characterized by a peak at 590 nm and a trough at 608 nm, that of species IIM by a peak at 606 nm, and that of species IIIM by a peak at 610 nm. A comparison with the difference spectra of species IIM and IIIM obtained with soluble cytochrome oxidase [Clore, Andréasson, Karlsson, Aasa & Malmström (1980) Biochem. J. 185, 155-167] revealed small but significant differences in the peak positions and bandwidths of the 605-610 nm absorption band.
D000818:Animals; D002248:Carbon Monoxide; D002417:Cattle; D003080:Cold Temperature; D003576:Electron Transport Complex IV / Q000378:metabolism*; D007425:Intracellular Membranes / Q000201:enzymology*; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology*; D010084:Oxidation-Reduction; D010100:Oxygen / Q000378:metabolism*; D011485:Protein Binding; D013053:Spectrophotometry / Q000379:methods
D002248:Carbon Monoxide; D003576:Electron Transport Complex IV; D010100:Oxygen