Bioenergetics pp 155-159 | Cite as

The Separation between Cytochrome A and Cytochrome A3 in the Absolute Spectrum

  • Taketomo Fujiwara
  • Yoshihiro Fukumori
  • Tateo Yamanaka


aa3-Type cytochrome was purified from Halobacterium halobium (1). The cytochrome contained two heme a molecules per molecule but no copper. It did not show cytochrome c oxidase activity. One of the two heme a molecules in the cytochrome was reduced with ascorbate + TMPD, while the other was not reduced with this reducing reagents. The heme a molecule reducible with ascorbate + TMPD did not react with CO, while the heme a molecule reducible only with Na2S2O4 reacted with CO. Therefore, cytochrome a. or heme aA in the cytochrome was separated from cytochrome a3 or heme aB on the reduction with ascorbate + TMPD; the γ peaks of ferrocytochrome a and ferricytochrome a3 were observed spectrophotometrically in the absolute spectrum. As CuA is known to be unnecessary for cytochrome aa3 to oxidize ferrocytochrome c (2), these results mentioned above show that copper atom, CuB mediate electrons between heme aA and heme aB.


Copper Atom Difference Spectrum Nitrosomonas Europaea Halobacterium Halobium Absolute Spectrum 
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  1. 1.
    Fujiwara, T., Fukumori, Y. and Yamanaka, T. (1989) J. Biochem. 105, 287–292.PubMedGoogle Scholar
  2. 2.
    Numata, M., Yamazaki, T., Fukumori, Y. and Yamanaka, T. (1989) J. Biochem. 105, 245–248.PubMedGoogle Scholar
  3. 3.
    Keilin, D. and Hartree, E.F. (1939) Pros. Roy. Soc. London, B127, 167–191.CrossRefGoogle Scholar
  4. 4.
    Okunuki, K., Sekuzu, I., Yonetani, T. and Takemori, S. (1958) J. Biochem. 45, 847–854.Google Scholar
  5. 5.
    Sekuzu, I., Takemori, S., Yonetani, T. and Okunuki, K. (1959) J. Biochem. 46, 43–49.Google Scholar
  6. 6.
    Okunuki, K. (1972) in Aspects of Cellular and Molecular Physiology (ed. by Hamaguchi, K.) University of Tokyo Press, Tokyo, pp. 57–73Google Scholar
  7. 7.
    Yonetani, T. (1960) J. Biol. Chem. 235, 845–852.PubMedGoogle Scholar
  8. 8.
    King, T.E. (1965) in Oxidases and Related Redox Systems (ed. by King, T.E., Mason, H.S. and Morrison, M.) Wiley, New York, p. 539.Google Scholar
  9. 9.
    Yamanaka, T., Kamita, Y. and Fukumori, Y. (1981) J. Biochem. 89, 265–273.PubMedGoogle Scholar
  10. 10.
    Ludwig, B. (1987) FEMS Microbiol. Rev. 46, 41–56.CrossRefGoogle Scholar
  11. 11.
    Wikstrom, M., Saraste, M. and Penttila, T. (1985) in The Enzymes of Biological Membranes (ed. by Martonosi, A.N.) Plenum, New York, vol. 4, pp. 111–148.Google Scholar
  12. 12.
    Yamanaka, T., Fukumori, Y., Yamazaki, T., Kato, H. and Nakayama, K. (1985) J. Inorg. Biochem. 23, 273–277.PubMedCrossRefGoogle Scholar
  13. 13.
    Fujiwara, T., Fukumori, Y. and Yamanaka, T. (1987) Plant Cell Physiol. 28, 29–36Google Scholar

Copyright information

© Plenum Press, New York 1990

Authors and Affiliations

  • Taketomo Fujiwara
    • 1
  • Yoshihiro Fukumori
    • 1
  • Tateo Yamanaka
    • 1
  1. 1.Department of Life Science, Faculty of ScienceTokyo Institute of TechnologyTokyo 152Japan

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