| Primary Source |
Abeles, R. H., Frey, P. A. and Jencks, W. P.: 1992, Biochemistry, Jones and Bartlett Publishers, Boston, pp. 91. AND Berg OG, von Hippel PH. Diffusion-controlled macromolecular interactions. Annu Rev Biophys Biophys Chem. 1985 14: 131-60 AND Eigen M, Hammes GG. Elementary steps in enzyme reactions (as studied by relaxation spectrometry). Adv Enzymol Relat Subj Biochem. 1963 25 :1-38 AND Fersht, A. 1985, Enzyme Structure and Mechanism, W. H. Freeman, New York, pp. 147–154 AND Moore, W. J.: 1983, Basic Physical Chemistry, Prentice-Hall, Inc., Englewood Cliffs NJ, pp. 348– 349.PubMed ID3890878, 14149678
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| Comments |
P.478 2nd paragraph: "At 25°C the maximum rate constant of an aqueous diffusion-controlled encounter for two reacting molecules is 10^9-10^11 M^-1×sec^-1 (primary sources Berg and von Hippel, 1985, Eigen and Hammes, 1963, Fersht, 1985), and for a molecule and an enzyme about 10^9 M^−1 Sec^−1 (primary sources Abeles et al., 1992a, Fersht, 1985, Moore, 1983c)." See BNID 103809, 103916 |