Kinetics: Enzymes and Electrons

  • Peter R. Bergethon


In the last chapter we discussed the general principles of kinetics and drew heavily on simple molecular interactions in a vacuum, in other words, gas behavior. This has allowed us to use kinetic theory to discuss the important abstraction of the potential energy surface. Yet most of the reactions of interest to the biologist and biophysical chemist occur in solution. We have drawn a fairly detailed picture of the molecular interactions that complicate the description and behavior of solutions. In general, the rate of a reaction in solution cannot occur any more rapidly than the rate of diffusion that brings the reactants together. Diffusion is the result of a chemical potential driving force that affects the motion of chemical species. We have also seen that the motion of ions in solution can be affected by externally applied electric fields. Finally we have explored how the electric field at the surfaces/solvent interface leads to the important transitional structure of the interphase. We will now see how the rates of surface (binding) reactions and electrochemical processes, which are extremely common in biological systems, are very sensitive to the electrical and chemical potentials at those surfaces.


Electron Transfer Potential Energy Surface Electrochemical Reaction Potential Energy Curve Reorganization Energy 
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.

Further Reading

Enzyme Kinetics

  1. Cantor C. R. and Schimmel P. R. (1980) Biophysical Chemistry, Part III. W. H. Freeman, New York.Google Scholar
  2. Stryer L. (1995) Biochemistry, 4th ed. W. H. Freeman, New York.Google Scholar
  3. Tinocco I., Sauer K., and Wang J. C. (1994) Physical Chemistry (Principles and Applications in the Biological Sciences), 3rd ed. Prentice-Hall, Engelwood Cliffs, NJ.Google Scholar

Aspects of Enzyme Kinetics

  1. Klinman J. P. (1978) Kinetic isotope effects in enzymology. Adv Enzym., 46: 415–94.Google Scholar
  2. Lerner R. A. and Tramontano A. (1988) Catalytic antibodies. Sci. Am., 258 (3): 58–70.PubMedCrossRefGoogle Scholar
  3. Natarajan K. R. (1991) Biocatalysis in organic solvents. J. Chem. Ed., 68: 13–16.CrossRefGoogle Scholar
  4. Slater E. C. (1981) Maxwell demons and enzymes. TIBS, Oct:280–1. The enzyme as a perpetual-motion machine?Google Scholar
  5. Walsh C. (1979) Enzymatic Reaction Mechanisms. W. H. Freeman, New York. This wonderful book is filled with descriptions of a wide variety of enzyme mechanisms. It is like a chemical gothic mystery filled with fascinating characters.Google Scholar

Dynamic Electrochemistry General

  1. Albery W. J. (1980) The application of the Marcus relation to reactions in solution. Ann. Rev. Phys. Chem., 31: 227–63.CrossRefGoogle Scholar
  2. Bockris J. O’M., and Reddy A. K. N. (1970) Modern Electrochemistry, vol. 2. Plenum, New York.CrossRefGoogle Scholar
  3. Faulkner L. R. (1983) Understanding electrochemistry: Some distinctive concepts. J. Chem. Ed., 60: 262–4.CrossRefGoogle Scholar
  4. Khan S. U., Kainthla R. C., and Bockris, J. O’M. (1987) The redox potential and the Fermi level in solution. J. Phys. Chem., 91: 5974–7.Google Scholar


  1. Evans D. H., O’Connell K. M., Petersen R. A., and Kelly M. J. (1983) Cyclic voltammetry. J. Chem. Ed., 60: 290–8.CrossRefGoogle Scholar
  2. Kissinger P. T., and Heineman W. R. (1983) Cyclic voltammetry. J. Chem. Ed., 60: 702–6.CrossRefGoogle Scholar

Biological Electron Transfer

  1. Beratan D. N., Betts J. N., and Onuchic J. N. (1991) Protein electron tunneling transfer rates set by the bridging secondary and tertiary structure. Science, 252: 1285–8.PubMedCrossRefGoogle Scholar
  2. Beratan D. N., Onuchic J. N., Winkler J. R., and Gray H. B. (1992) Electron tunneling paths in proteins. Science, 258: 1740–1.PubMedCrossRefGoogle Scholar
  3. Boxer S. G. (1990) Mechanisms of long-distance electron transfer in proteins: Lessons from photosynthetic reaction centers. Ann. Rev. Biophys. Biophys. Chem., 19: 267–99.CrossRefGoogle Scholar
  4. Gray H. B., and Winkler J. R. (1996) Electron transfer in proteins. Ann. Rev. Biochem., 65: 537–61.PubMedCrossRefGoogle Scholar
  5. Khan S. U. (1988) Models of electron transfer reactions at a biological-membrane covered electrode-solution interface. J. Phys. Chem., 92: 2541–6.CrossRefGoogle Scholar
  6. Kuki A., and Wolynes P. G. (1987) Electron tunneling paths in proteins. Science, 236: 1647–52.PubMedCrossRefGoogle Scholar
  7. Moser C. C., Keske J. M., Warncke K., Farid R. S. and Dutton P. L. (1992) Nature of biological electron transfer. Nature, 355: 796–802.PubMedCrossRefGoogle Scholar
  8. Onuchic J. N., Beratan D. N., Winkler J. R., and Gray H. B. (1992) Pathway analysis of protein electron-transfer reactions. Ann. Rev. Biophys. Biomol. Struct., 21: 349–77.CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Peter R. Bergethon
    • 1
  1. 1.Department of BiochemistryBoston University School of MedicineBostonUSA

Personalised recommendations