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Studies on Cytochrome Oxidase
Open accessAbstract
SUMMARY The oxidation of the half-reduced cyanide complex of cytochrome oxidase (a2+. Cu’+. aa3+CN) by ferricyanide showed a one to one correlation between the formation of the 830-nm absorption band and the generation of the EPR Cu(II) signal at g = 2. Both required 1.0 mole of ferricyanide per mole of cytochrome oxidase of 4 oxidation equivalents. On the other hand, the titration measured at 603 nm required 2.4 moles of oxidant; the fractional ratio apparently resulted from absorbance contribution by the Cu(I1) chromophore. The titration curves measured at 830 nm and by EPR for the fully reduced cyanide complex (a2+. Cul+. a3%!N) were sigmoidal. These and other observations suggest that significant heme-copper interaction exists between the EPR-sensitive copper chromophore and cytochrome a on one hand and cytochrome a3 on the other. Structurally and functionally the EPR-sensitive copper which shows the 830-nm absorption band is most likely to be sandwiched between cytochromes (I and a3, whereas the
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Cited by
Studies on Cytochrome c Peroxidase
Yonetani, T. (1965) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)97091-2 · Cited by 278
Self-citationMercer, S. W., & Trayhurn, P. (1987) · The Journal of Nutrition · doi:10.1093/jn/117.12.2147 · Cited by 146
Metadata
- Authors
- Yonetani, T., & Ray, G. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1965-08
- Volume
- 240
- Issue
- 8
- Pages
- 3392-3398
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2403196200
- Cited by
- 326
- References
- 0
- FWCI
- 11.64
- Type
- journal article
- Language
- en
- Open access
- hybrid
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