Abstract
PREVIOUSLY it has been generally believed that the substrates of the cytochrome oxidase system, such as p-phenylene diamine and hydroquinone, are only oxidized by cytochrome oxidase through cytochrome c. However, since p-phenylene diamine is fairly well oxidized by particulate cytochrome oxidase preparations in the absence of cytochrome c, whereas the other substrates, such as hydroquinone are not, Okunuki1 has suggested that the reductant of the so-called Nadi-reaction can reduce not only cytochrome c but also cytochrome oxidase. This was confirmed spectrophotometrically by Smith2.
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References
Okunuki, K., Acta Phytochim., 12, 1 (1941).
Smith, L., J. Biol. Chem., 215, 837 (1955).
Okunuki, K., Hagihara, B., Sekuzu, I., and Horio, T., Internat. Symp. Enz. Chem., Paper No. 227 (1957). Okunuki, K., Sekuzu, I., Yonetani, T., and Takemori, S., J. Biochem. (Japan) (in the press). Sekuzu, I., Takemori, S., Yonetani, T., and Okunuki, K., ibid. (in the press).
Yonetani, T., Takemori, S., Sekuzu, I., and Okunuki, K., Nature, 181, 1339 (1958).
Yakushiji, E., and Okunuki, K., Proc. Imp. Acad. Japan, 16, 229 (1940).
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TAKEMORI, S., SEKUZU, I., YONETANI, T. et al. Reconstruction of the Reaction Mechanism of Cytochrome Oxidase. Nature 182, 1306–1307 (1958). https://doi.org/10.1038/1821306a0
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DOI: https://doi.org/10.1038/1821306a0
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