Skip to main content

The Reaction of Oxygen with Cytochrome Oxidase: The Role of Sequestered Intermediates

  • Conference paper
Oxygen and Living Processes

Part of the book series: Topics in Environmental Physiology and Medicine ((TEPHY))

Abstract

Cytochrome oxidase is specifically served by oxygen delivery from the blood, and affords the main energy conservation pathway of the eukaryotic cell. The mechanism by which cytochrome oxidase reduces to water the total oxygen delivery and affords efficient production of ATP without production of toxic intermediates of oxygen reduction is one of the principal problems of modern biochemistry, on which significant advances have been made recently. The quantitation of structural and functional features of cytochrome oxidase has been obtained by low dose electron microscopy, low angle diffraction from oriented bilayers, and most recently anomalous scattering. These approaches are complemented by low temperature kinetics and sensitive spectrophotometry to afford a “first step” toward the correlation of structural and functional aspects of cytochrome oxidase and the cytochrome oxidase-oxygen reaction mechanism.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Chance, B., Waring, A., and Saronio, C. (1978). Low temperature transport in cytochrome c in the cytochrome c-cytochrome oxidase reaction: Evidence for electron tunneling. 29 Colloquium der Gesellschaft fur Biologische Chemie 6–8 April 1978, Mos- bach, Baden. In: Schafer, G., and Klingen- berg, M. (Eds.). Energy Conservation in Biological Membranes. Berlin: Springer- Verlag, pp. 56–73.

    Google Scholar 

  2. Chance, B., Waring, A., and Yang, E. (1979). Interaction of electron doners and soluble cytochrome oxidase at intermediate- low temperatures. Biophys. J. 25: 44a.

    Google Scholar 

  3. Chance, B. Waring, A., and Powers, L. (1979). The role of peroxidase-like intermed-iates in the enzymatic function of cytochrome oxidase over a variety of temperatures. Proceedings of the Japanese-American Seminar on Cytochrome Oxidase, Kobe, Japan, 1978. New York: Elsevier/North Holland, pp. 353–360.

    Google Scholar 

  4. Powers, L. Blumberg, W., Ching, Y., Eisen- berger, P., Chance, B., Barlow, C., Leigh, J. S., Jr., Smith, J., Yonetani, T., Peisach, J., Vik, S., Hastings, B., and Perlman, M. (1979). X-ray absorption edge and extended fine structure (EXAFS) studies on cytochrome c oxidase. Biophys. J. 25 (2): 43a.

    Google Scholar 

  5. Hu, V. W., Chan, S. I., and Brown, G. (1977). X-ray absorption edge studies on cyanide-bound cytochrome c oxidase. FEBS Lett. 84: 287–290.

    Article  PubMed  CAS  Google Scholar 

  6. Chance, B., and Leigh, J. S., Jr. (1977). Oxygen intermediates and mixed valence states of cytochrome oxidase: Infrared ab-sorption difference spectra of compounds A, B, and C of cytochrome oxidase and oxygen. Proc. Natl. Acad. Sci. U.S.A. 74: 4777–4780.

    Google Scholar 

  7. Chance, B., Saronio, C., and Leigh, J. S., Jr. (1979). Compound C2—a product of the reaction of oxygen and the mixed valence state of cytochrome oxidase: Optical evi-dence for a type I copper. Biochem. J. 177: 931–941.

    PubMed  CAS  Google Scholar 

  8. Powers, L., Blumberg, W., Chance, B., Barlow, C., Leigh, J. S., Jr., Smith, J., Yonetani, T., Vik, S., and Peisach, J. (1979). The nature of copper atoms of cytochrome c oxidase as studied by optical and x-ray absorption edge spectroscopy. Biochem. Bio- phys. Acta. 546: 520–538.

    Article  CAS  Google Scholar 

  9. Brown, J. M. (1978). Dissertation, Department of Chemistry. Princeton University.

    Google Scholar 

  10. Brown, J. M., Powers, L., Kincaid, B., Larrabee, J. A., and Spiro, T. (1980). Structural studies of the hemocyanin active site. I. EXAFS (extended x-ray absorption fine structure) analysis. J. Am. Chem. Soc. 102 (2): 4210–4216.

    Article  CAS  Google Scholar 

  11. Alben, J. O., Altschuld, F., and Moh, P. (1981). Structure of the cytochrome oxidase (a3) heme pocket. Low temperature FTIR spectroscopy of the photolyzed CO complex. In: Ho, Chien (Ed.). Interaction between Iron and Proteins in Oxygen and Electron Transport. New York: Elsevier/North Holland. In press.

    Google Scholar 

  12. Chance, B., Angiolillo, P., Yang, E., and Powers, L. (1980). Identification and assay of synchrotron radiation-induced alterations on metalloenzymes and proteins. FEBS Lett. 112 (2): 178–182.

    Article  PubMed  CAS  Google Scholar 

  13. DeVault, D., and Chance, B. (1966). Studies of photosynthesis using a pulsed laser. Bio- phys. J. 6 (6): 825–847.

    CAS  Google Scholar 

  14. Wikstrom, M. (1980). Mechanism of proton translocation by mammalian cytochrome oxidase. First European Bionergetics Conference, Urbino, Italy.

    Google Scholar 

  15. Chance, B., Gibson, Q., Eisenhardt, R., and Lonberg-Holn, K. (1964). Rapid mixing and sampling techniques as applied to biochemical kinetics. Science 146: 3652.

    Google Scholar 

  16. Chance, B. Possible structures of cytochrome oxidase-oxygen intermediates and their reactivity toward cytochrome c. In: Lee, C. P. Schatz, G., Ernster, L. (Eds.). Membrane Bioenergetics. Reading, Massachusetts: Addison Wesley, pp. 1–12.

    Google Scholar 

  17. Chance, B. (1943). The kinetics of the enzymatic substrate compound of peroxidase. J. Biol. Chem. 151: 553–557.

    Google Scholar 

  18. Chance, B., Azzi, A., Lee, I., Lee, C. P., and Mela, L. (1968). In: Ernster, L., and Drahota, Z. (Eds.). Mitochondria: Structure and Function. London: Academic Press, FEBS Symp. 17: 233.

    Google Scholar 

  19. Capaldi, R. (1981). Structure and function of cytochrome oxidase. In: Ho, Chien (Ed.). Interaction between Iron and Proteins in Oxygen and Electron Transport. New York: Elsevier/North Holland. In press.

    Google Scholar 

  20. Frey, T. (1978). Structure and orientation of cytochrome c oxidase in crystalline membranes. J. Biol. Chem. 253: 4389–4395.

    PubMed  CAS  Google Scholar 

  21. Henderson, R., Capaldi, R, and Leigh, J. S., Jr. (1977): Arrangement of cytochrome oxidase molecules in two dimensional vesicle crystals. J. Mol. Biol. 112: 631–648.

    Article  PubMed  CAS  Google Scholar 

  22. Weiss, H., Wingfield, P., Leonard, K., Winkler, F., Perkins, S., and Miller, A. (1980). Structure of ubiquinone: Cytochrome c reductase from neurospora mitochondria. First European Biogenetics Conference, Urbino, Italy.

    Google Scholar 

  23. Blasie, J. K., and Stamatoff, J. (1981). The use of resonance x-ray scattering for determining spatial relationships among metal atoms within macromolecules in noncrystalline state. Ann. Rev. Biophys. Bioeng. In press.

    Google Scholar 

  24. Ludwig, B., and Schatz, G. (1980). Two subunit cytochrome c oxidase (cytochrome aa3) from Paracoccus denitrificans. Proc. Natl. Acad. Sei. U.S.A. 77 (1): 196–200.

    Article  CAS  Google Scholar 

  25. Sone, N., Ohyama, T., and Kagaway, Y. (1979) Thermostable single-band cytochrome oxidase. FEBS Lett. 106 (l): 39–42.

    Article  PubMed  CAS  Google Scholar 

  26. Chance, B., Crofts, A., Nishimura, N., and Price, B. (1970), Fast membrane H+ binding in the light-activated state of Chromatium chromatophores. Eur. J. Biochem. 13: 364–374.

    Article  Google Scholar 

  27. Chance, B. (1981). Oxygen transport and oxygen reduction. In: Ho, Chien (Ed.). Interaction between Iron and Proteins and Electron Transport. New York: Elsevier/ North Holland. In press.

    Google Scholar 

Download references

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1981 Springer-Verlag New York, Inc.

About this paper

Cite this paper

Chance, B. (1981). The Reaction of Oxygen with Cytochrome Oxidase: The Role of Sequestered Intermediates. In: Gilbert, D.L. (eds) Oxygen and Living Processes. Topics in Environmental Physiology and Medicine. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-5890-2_10

Download citation

  • DOI: https://doi.org/10.1007/978-1-4612-5890-2_10

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-5892-6

  • Online ISBN: 978-1-4612-5890-2

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics