Maximum rate constant of an aqueous diffusion-controlled encounter for a molecule and enzyme at 25˚C

Range 10^9 to 10^11 M^-1×sec^-1
Organism Generic
Reference Weber AL. Kinetics of organic transformations under mild aqueous conditions: implications for the origin of life and its metabolism. Orig Life Evol Biosph. 2004 Oct34(5):473-95. p.478 2nd paragraphPubMed ID15573498
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
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
Entered by Uri M
ID 106505