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In a third experiment, this time at -50°, the formation of Compound B is indicated by the unresolved abrupt downward deflection of the trace at 605 nm, occurring in a few tenths of a second. There is, however, a slower phase of the reaction which is not complete within the scale of the recording that we attribute to the slow oxidation of cytochrome a. In order to observe the completion of the reaction, the experiment is repeated for a fourth time at -20°, where the oxidation of cytochrome oxidase is complete in a fraction of the 200 msec time marker.

P. 295. , Ltd. Chance, B. U959a). J. Biol. Chem. 224, 3036-3040. Chance, B. (1959b). J. Biol. Chem. 234, 3041-3043. , Estabrook, R. , and Ghosh, A. (1964). Proc. Nat'I. Acad. , USA 51, 1244-1251. , and Hess, B. (1959). J. Biol. Chem. 234, 24042412. , MacNichol, E. , and Williams, F. C. (1964). "Waveforms, MIT Rad. Lab. Series," Vol. XIX. Boston Tech. , Lexington, Massachusetts. , Pye, E. , Ghosh, A. , and Hess, B. (1973). " Academic Press, New York. , and Leigh, J. S. Bioohim. Biophys. Acta, in press.

1976). Further evidence for the separate nature of the two parts of cytochrome oxidase is indicated by its reaction with oxygen to form Compound C (see Fig. 16) as is illustrated by Fig. 23. The initial state (Spectrum A) is the same as that of Fig. , the fully reduced state obtained as before by flash photo- Oxygen Metabolism in Yeast Cells 43 Wavelength (nm) CS 10a FIGURE 22. Effect of various treatments upon the split a band of cytochrome oxidase in Candida utitis cells¿ trace A oxidized minus reduced at room temperature.

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