Journal of Molecular Evolution

, Volume 1, Issue 1, pp 26–45 | Cite as

The structure of cytochromec and the rates of molecular evolution

  • Richard E. Dickerson


The x-ray structure analysis of ferricytochromec shows the reasons for the evolutionary conservatism of hydrophobic and aromatic side chains, lysines, and glycines, which had been observed from comparisons of amino acid sequences from over 30 species. It also shows that the negative character of one portion of the molecular surface is conserved, even though individual acidic side chains are not, and that positive charges are localized around two hydrophobic “channels” leading from the interior to the surface.

The reason for the unusual evolutionary conservation of surface features in cytochromesc is probably the interaction of the molecule with two other large macromolecular complexes, its reductase and oxidase. This conservation of surface structure also explains the relatively slow rate of change of cytochromec sequences in comparison with the globins and enzymes of similar size.

The rate of evolution of a protein is the rate of occurrence of mutations in the genome modified by the probability that a random change in amino acid sequence will be tolerable in a functioning protein. The observed rates of change in fibrinopeptides, the globins, cytochromec, and several enzymes are interpreted in terms of the proteins' biological roles.


Cytochromec Evolutionary Rates and Molecular Structure 


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  1. 1.
    Bradshaw, R. A., Neurath, H., Tye, R. W., Walsh, K. A., Winter, W. P.: Nature (Lond.)226, 237 (1970).Google Scholar
  2. 2.
    Chance, R. E., Ellis, R. M., Bromer, W. W.: Science161, 165 (1968).Google Scholar
  3. 3.
    Dayhoff, M. O.: Atlas of protein sequence 1969. Silver Spring, Maryland: Nat. Biomed. Res. Found. 1969.Google Scholar
  4. 4.
    DeLange, R. J., Fambrough, D., Smith, E. L., Bonner, J.: J. biol. Chem.244, 5669 (1969).Google Scholar
  5. 5.
    Dickerson, R. E., Geis. I.: The structure and action of proteins. New York: Harper & Row 1969.Google Scholar
  6. 6.
    —, Takano, T., Eisenberg, D., Kallai, O. B., Samson, L., Cooper, A., Margoliash, E.: J. biol. Chem.246, 1511 (1971).Google Scholar
  7. 7.
    - - Kallai, O. B., Samson, L.: Proceedings of the Wenner-Gren Symposium on Oxidation-Reduction Enzymes. Stockholm, August 1970. In press.Google Scholar
  8. 8.
    Fitch, W. M., Margoliash, E.: Science155, 279 (1967).Google Scholar
  9. 9.
    Glaessner, M. F.: Earth Sci. Rev.1, 29 (1966).Google Scholar
  10. 10.
    Ingram, V. M.: The hemoglobins in genetics and evolution. New York: Columbia U.P. 1963.Google Scholar
  11. 11.
    King, J. L., Jukes, T. H.: Science164, 788 (1969).Google Scholar
  12. 12.
    Kulp, J. L.: Science133, 1105 (1961).Google Scholar
  13. 13.
    Margoliash, E.: Proc. nat. Acad. Sci. (Wash.)50, 672 (1963).Google Scholar
  14. 14.
    —, Fitch, W. M.: Ann. N.Y. Acad. Sci.151, 359 (1968).Google Scholar
  15. 15.
    —, —, Dickerson, R. E.: Brook. Symp. Biol.21, 259 (1968).Google Scholar
  16. 16.
    —, Smith, E. L.: In: Evolving genes and proteins (V. Bryson and H. J. Vogel, eds.). New York: Academic Press 1965.Google Scholar
  17. 17.
    Mross, G. A., Dolittle, R. F.: Arch. Biochem.122, 674 (1967).Google Scholar
  18. 18.
    Nolan, C., Margoliash, E.: Ann. Rev. Biochem.37, 727 (1968).Google Scholar
  19. 19.
    Romer, A. S.: The vertebrate body, 3rd ed. Philadelphia: Saunders 1962.Google Scholar
  20. 20.
    —, The vertebrate story. Chicago: Univ. Chicago Press 1962.Google Scholar
  21. 21.
    Szalay, F. S.: Evolution22, 19 (1968).Google Scholar
  22. 22.
    Young, J. Z.: The life of vertebrates, 2nd ed. Oxford: Univ. Press 1962.Google Scholar
  23. 23.
    Zuckerkandl, E.: Sci. Amer.212, 110 (1965).Google Scholar
  24. 24.
    —, Pauling, L.: In: Evolving genes and proteins. (V. Bryson and H. J. Vogel, eds.) New York: Academic Press 1965.Google Scholar

Copyright information

© Springer-Verlag 1971

Authors and Affiliations

  • Richard E. Dickerson
    • 1
    • 2
  1. 1.Norman W. Church Laboratory of Chemical BiologyCalifornia Institute of TechnologyPasadenaUSA
  2. 2.Division of Chemistry and Chemical EngineeringCalifornia Institute of TechnologyPasadenaUSA

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