The Energy Dependent Redox Responses of Heme And Copper in Cytochrome Oxidase in Rat Brain In Situ

  • A. Matsunaga
  • Y. Nomura
  • M. Tamura
  • N. Yoshimura
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 388)


With the in vitro calibration of isolated mitochondria, it has been shown that the redox state of heme a+a3 in cytochrome oxidase depends on both mitochondrial energy state and respiratory rate, but that of copper does not (1,2, 3). This finding, however, has not been confirmed in vivo living tissues, since hemoglobin absorption masks the redox change of heme a+a3 in the visible region.


Cytochrome Oxidase Cerebral Tissue Redox Behavior Rapid Phase Redox Level 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Hoshi Y., Hazeki O., and Tamura M., 1989, The oxygen dependency of the redox state of heme and copper in cytochrome oxidase in vitro, Adv. Exp. Med. Biol. 248: 71–76.PubMedGoogle Scholar
  2. 2.
    Oshino N., Sugano T., and Chance B.,1974, Mitochondrial function under hypoxic conditions: the steady states of cytochrome a+a3 and their relation to mitochondrial energy states, Biochim. Biophys. Acta. 368: 298–310.PubMedCrossRefGoogle Scholar
  3. 3.
    Hoshi Y., Hazeki O., and Tamura M., 1993, Oxygen dependence of redox state of copper in cytochrome oxidase in vitro, J. Appi. Physiol. 74: 1622–1627.Google Scholar
  4. 4.
    Green Cross Crop., 1976, FC-43 Emulsion, Technical information Ser. No.3 September 4, Osaka.Google Scholar
  5. 5.
    Hlinak Z., and Madlafousek J., 1987, Transition from precopulatory to copulatory behavior in male rats with lesions in medial preoptic area, Act. Nerv. Super. 29: 257–262.Google Scholar
  6. 6.
    Andjus R.K., and Suhara K., 1967, An isolated, perfused rat brain preparation, its spontaneous and stimulated activity, J. Appi. Physiol. 22:1033–1039.Google Scholar
  7. 7.
    Inagaki M., and Tamura M., 1993, Preparation and optical characteristics of hemoglobin-free isolated perfused rat head in situ. J. Biochem. 113: 650–657.PubMedGoogle Scholar
  8. 8.
    Rich P.R., and West I.C., 1988, The location of CuA in mammalian cytochrome c oxidase, FEBS Lett. 233: 25–30.PubMedCrossRefGoogle Scholar
  9. 9.
    Lindsay J.G., and Wilson D.F., 1972, Apparent adenosine triphosphate induced ligand changes in cytochrome a3 of pigeon heart mitochondria, Biochemistry 11: 4613–4621.PubMedCrossRefGoogle Scholar
  10. 10.
    Wilson D.F., and Dutton P.L., 1970, The oxidation-reduction potentials of cytochromes a and a3 in intact rat liver mitochondria, Arch. Biochem. Biophys. 163: 583–584.CrossRefGoogle Scholar
  11. 11.
    Kariman K., and Burkhart D.S., 1985, Heme-copper relationship of cytochrome oxidase in rat brain in situ, Biochem. Biophys. Res. Commun. 126: 1022–1028.PubMedCrossRefGoogle Scholar
  12. 12.
    Hazeki O., and Tamura M., 1989, Near infrared quadruple wavelength spectrophotometry of the rat brain, Adv. Exp. Med. Biol. 247: 63–69.Google Scholar
  13. 13.
    Hoshi Y, and Tamura M., 1993, Dynamic changes in cerebral oxygenation in chemically induced seizures in rats: study by near-infrared spectrophotometry, Brain Res. 603: 215–221.PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1996

Authors and Affiliations

  • A. Matsunaga
    • 1
    • 2
  • Y. Nomura
    • 1
  • M. Tamura
    • 1
  • N. Yoshimura
    • 2
  1. 1.Research Institute for Electronic ScienceHokkaido UniversitySapporoJapan
  2. 2.Department of AnesthesiologyKagoshima University School of MedicineKagoshimaJapan

Personalised recommendations