Biochemistry pp 293-315 | Cite as

Electron Transport and Oxidative Phosphorylation

  • J. Stenesh


Free energy changes of chemical reactions are related to a number of parameters: entropy and enthalpy changes (Eq. 9.1), equilibrium constants (Eq. 9.2), and oxidation-reduction potentials. Of these, equilibrium constants and oxidation-reduction potentials are of primary importance for computing free energy changes of metabolic reactions. Relationships between free energy changes and equilibrium constants were explored in Chapter 9. Now we will focus on the relationships between free energy changes and oxidation-reduction potentials.


Oxidative Phosphorylation Cytochrome Oxidase Free Energy Change Electron Carrier Citric Acid Cycle 
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Selected Readings

  1. Abrahams, J. P., Leslie, A. G. W., Lutter, R., and Walker, J. E., Structure at 2.8À resolution of F1-ATPase from bovine heart mitochondria, Nature (London) 370: 621–628 (1994).CrossRefGoogle Scholar
  2. Bensasson, R. V., Land, E. J., and Truscott, T. G., Excited States and Free Radicals in Biology and Medicine, Oxford University Press, Oxford (1993).Google Scholar
  3. Fetter, J. R., et al.,Possible proton relay pathways in cytochrome c oxidase, Proc. Natl. Acad Sci. USA 92:1604–1608 (1995).Google Scholar
  4. Fridovich, I., Superoxide radical and superoxide dismutases, Annu. Rev. Biochem. 64: 97–112 (1995).PubMedCrossRefGoogle Scholar
  5. Gray, H. B., and Winkler, J. R., Electron transfer in proteins, Annu. Rev. Biochem. 65: 537–561 (1996).PubMedCrossRefGoogle Scholar
  6. Mitchell, P., Keilin’s respiratory chain concept and its chemiosmotic consequences, Science 206: 1148–1159 (1979).PubMedCrossRefGoogle Scholar
  7. Musser, S. M., and Stowell, M. H. B., Cytochrome c oxidase: Chemistry of a molecular machine, Adv. Enzymol. Relat. Areas Mol. Biol. 71: 79–208 (1995).PubMedGoogle Scholar
  8. Pedersen, P. L., and Amzel, L. M., ATP synthases: Structure, reaction center, mechanism, and regulation of one of nature’s most unique machines, J. Biol. Chem. 268: 9937–9940 (1993).PubMedGoogle Scholar
  9. Racker, E., From Pasteur to Mitchell: A hundred years of bioenergetics, Fed. Proc. 39: 210–215 (1980).PubMedGoogle Scholar
  10. Rees, D. C., and Farrelly, D., Biological electron transfer, in The Enzymes, 3rd ed. (D. S. Sigman and P. D. Boyer, eds.), Vol. 19, pp. 38–97, Academic Press, New York (1990).Google Scholar
  11. Stenesh, J., Core Topics in Biochemistry, Cogno Press, Kalamazoo, MI (1993).Google Scholar
  12. Trumpower, B. L., and Gennis, R. B., Energy transduction by cytochrome complexes in mitochondria) and bacterial respiration: The enzymology of coupling electron transfer reactions to trans-membrane proton translocation, Annu. Rev. Biochem. 63: 675–716 (1994).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • J. Stenesh
    • 1
  1. 1.Western Michigan UniversityKalamazooUSA

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