About 47 years ago a very important paper on the rate of diffusion-controlled reactions of enzyme was published. According to its deduction, the upper limit of enzyme-substrate reaction is 1010/Msec, which is one order of magnitude higher than the conventional estimation by Manfred Eigen, who won the 1967 Nobel Prize in Chemistry for the work on measuring fast chemical reactions.
The new upper limit has been confirmed by a series of follow-up studies [1,2,3,4,5,6,7,8,9,10,11,12].
It is indeed very significant and profound for such a breakthrough or revolution in enzyme fast reaction. Particularly, it has also been supported by the eight masterpiece papers of the then Chairman of the Nobel Prize Committee (see, e.g.., [8,9;13,14,10,14].
Chou K.C. Studies on the enzyme kinetics of the cavity-active site. Acta Biochimica Biophysica Sin 7.95 (1975): 103.
Chou K.C. The kinetics of the combination reaction between enzyme and substrate. Scientia Sinica 19 (1976): 505–528.
Li T.T., and Chou K.C. The quantitative relations between diffusion-controlled reaction rate and characteristic parameters in enzyme–substrate reaction systems. I. Neutral substrates. Scientia Sinica 19.1 (1976): 117–136.
Chou K.C. The kinetics of the combination reaction between enzyme and substrate: 1. Stochastic analysis, activation energy and multiple-active-site. Acta Biochimica et Biophysica Sinica 9 (1977): 79–94.
Chou K.C. The kinetics of the combination reaction between enzyme and substrate: 2. Multi-barrier reaction and measuring signal. Acta Biochimica et Biophysica Sinica 9 (1977): 175–186.
Li T.T., and Chou K.C. Studies on the combination rates of liquid phase fast reaction systems—steady state process and transient phase process. Scientia Sinica 20.2 (1977): 197–221.
Zhou G. Influences of Van der Waals. Scientia Sinica 22.7 (1979): 845–858.
Chou K.C., and Forsén S. Diffusion-controlled effects in reversible enzymatic fast reaction systems—critical spherical shell and proximity rate constant. Biophysical Chemistry 12.3–4 (1980): 255–263.
Li T.T. and Chou K.C. The flow of substrate molecules in fast enzyme-catalyzed reaction systems. Chemica Scripta 16.5 (1980): 192–196.
Chou K.C. et al. The biological functions of low-frequency phonons. 2. Cooperative effects. Chemica Scripta 18.3 (1981): 126–132.
Zhou G.Q., and Zhong W.Z. Diffusion-controlled reactions of enzymes: A comparison between Chou's model and Alberty–Hammes–Eigen's model. European Journal of Biochemistry 128.2–3 (1982): 383–387.
Payens T.A.J. Why are enzymes so large? Trends in Biochemical Sciences 8.2 (1983): 46.
Chou K.C., and Forsén S. Graphical rules for enzyme-catalysed rate laws. Biochemical Journal 187.3 (1980): 829–835.
Chou K.C., and Forsén S. Graphical rules of steady-state reaction systems. Canadian Journal of Chemistry 59.4 (1981): 737–755.
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