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Enzyme Catalysis: The View from Physical Chemistry

  • Alan Cooper
  • Julien L. Houben
Part of the Progress in Mathematics book series (NSSA)

Abstract

The role of an introductory lecturer is a difficult one. There is a quite natural human temptation to attempt to appear erudite and profound about the subject, but this must be balanced by an awareness of the diverse backgrounds and different areas of specialisation of the audience. Even though we all share a common scientific language (expressed in various degrees of “fractured English”), there are many dialects associated with the various sub-disciplines (physics, chemistry, biology...) which can make communication difficult. This introductory lecture, therefore, is merely an attempt to set the scene for what what follows and to establish some common ground. But we should caution from the start that the title might mislead one into the belief that there is an agreed consensus concerning the understanding of enzyme catalysis from the physico-chemical point of view. This is not the case, and no such global understanding exists. Indeed, if it did, then there would be no need for a meeting such as this. This is a healthy situation indicative of the intellectual excitement and practical importance of the topic in current times when biotechnology offers so much promise. So, in what follows, we do not pretend to give any comprehensive view of the physical chemistry of enzyme catalysis, rather we will present a series of basic ideas — some well established and others rather less so, some abstruse and some trivial — which will form a backcloth for the more detailed lectures that follow. Few, if any, of these observations will be original, and further details and background references may be found in the Bibliography at the end of this chapter.

Keywords

Enzyme Catalysis Rate Enhancement Enzyme Active Site Energy Fluctuation Active Site Cleft 
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.

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References

  1. 1.
    A.R. Fersht, “Enzyme Structure and Mechanism”, W.H. Freeman, San Francisco (1985).Google Scholar
  2. 2.
    W.P. Jencks, “Catalysis in Chemistry and Enzymology”, McGraw-Hill, New York (1969).Google Scholar
  3. 3.
    J. Kraut, “How Do Enzymes Work ?”, Science 242, 533–540 (1988).PubMedCrossRefGoogle Scholar
  4. 4.
    M.I. Page (editor), “The Chemistry of Enzyme Action”, Elsevier, Amsterdam (1984).Google Scholar
  5. 5.
    M.I. Page & A. Williams, “Enzyme Mechanisms”, Royal Society of Chemistry, London (1987).Google Scholar
  6. 6.
    A. Cooper, “Protein Fluctuations and the Thermodynamic Uncertainty Principle”, Progr.Biophys.Mol.Biol. 44, 181–214 (1984).CrossRefGoogle Scholar
  7. 7.
    J.A. McCammon & S.C. Harvey, “Dynamics of Proteins and Nucleic Acids”, Cambridge University Press, Cambridge (1987).CrossRefGoogle Scholar
  8. 8.
    B.Somogyi, G.R.Welch & S.Damjanovich, “The Dynamic Basis of Energy Transduction in Enzymes”, Biochim.Biophys.Acta 768, 81–112 (1984).PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1989

Authors and Affiliations

  • Alan Cooper
    • 1
  • Julien L. Houben
    • 2
  1. 1.Department of ChemistryGlasgow UniversityGlasgowScotland, UK
  2. 2.Istituto di Chimica Quantistica ed Energetica Molecolaré CNRPisaItaly

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