Reactions of cytochrome oxidase.
نویسنده
چکیده
In 1939 Keilin and Hartree (2) advanced the concept that there are two cytochrome components reacting between cytochrome c and oxygen; namely, cytochrome a and cytochrome a3. They based their hypothesis principally on the action of carbon monoxide which caused the a-band of reduced cytochrome a to spread toward 590 rnp and the r-band at 448 rnp to shift to 430 rnp and to be replaced by a very pale band at 452 ml*. They felt that their studies with other inhibitors, and especially with cyanide, skengthened their position. Under anaerobic conditions KCN broadened the a-band of reduced cytochrome a toward the blue end of the spectrum and broadened and slightly shifted the r-band toward the red end of the spectrum. In other experiments, however, in which the succinate was added in the presence of air, the a-band remained unchanged, while the y-band disappeared and was replaced by a pale band at 452 mp. The effect of cyanide on the spectrum of oxidized cytochrome oxidase has been noted by Smith (3) and by Ball and Cooper (4), whereas the effect on the spectrum of the reduced enzyme has been reported by a number of investigators (2-6). The effect of CO on the spectrum of reduced cytochrome oxidase was studied in detail by Warburg and his associates (7, 8) when they determined the photochemical action spectrum of the CO compound of the enzyme in yeast. Other investigators have amply confirmed the action of CO (2, 5, 6, 9-11). In this paper it is shown that NaCN modifies the spectra of both oxidized and reduced cytochrome 0xidase.r CO is shown to affect the spec-
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ورودعنوان ژورنال:
- The Journal of biological chemistry
دوره 212 2 شماره
صفحات -
تاریخ انتشار 1955