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Title: 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. Author: Clore GM. Journal: Biochem J; 1980 Jun 01; 187(3):617-22. PubMed ID: 6331384. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]