Literature DB >> 1273571

The quantitative relations between diffusion-controlled reaction rate and characteristic parameters in enzyme-substrate reaction systems. I. Neutral substrates.

T T Li, K C Chou.   

Abstract

With the development of techniques for studying fast reactions, we are confronted with some experimental observations which, according to the classical diffusion-controlled reaction theory based on the assumption of pherical symmetry, will lead to paradoxical consequences. Recently, some investigators have attempted to present a theory of non-spherically symmetric diffusion-controlled reaction. Owing to the difficulty in mathematics, only the formal discussion has been given, and the numerical results have not yet been reported. The combination between enzyme and substrate is not only non-spherically symmetric, but also related to the force field existing between the reacting molecules. In the previous article we introduced the spatial factor and the force field factor and derived a general equation for these reaction systems. We present in this article a general method for finding the numerical solution of the above equation. With the numerical results obtained by this method we may interpret the experimental facts which can not be explained from the viewpoint of the classical diffusion-controlled reaction theory. In order to examine more closely the kinetic behaviour of enzyme-substrate reaction systems, we defined several characteristic parameters. The quantitative relation between these parameters and the rate of diffusion-controlled reaction has been discussed.

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Year:  1976        PMID: 1273571

Source DB:  PubMed          Journal:  Sci Sin        ISSN: 0250-7870


  6 in total

1.  Evolution of enzyme catalytic power. Characteristics of optimal catalysis evaluated for the simplest plausible kinetic model.

Authors:  K Brocklehurst
Journal:  Biochem J       Date:  1977-04-01       Impact factor: 3.857

2.  The pH-dependence of second-order rate constants of enzyme modification may provide free-reactant pKa values.

Authors:  K Brocklehurst; H B Dixon
Journal:  Biochem J       Date:  1977-12-01       Impact factor: 3.857

3.  The equilibrium assumption is valid for the kinetic treatment of most time-dependent protein-modification reactions.

Authors:  K Brocklehurst
Journal:  Biochem J       Date:  1979-09-01       Impact factor: 3.857

4.  Different Anomeric Sugar Bound States of Maltose Binding Protein Resolved by a Cytolysin A Nanopore Tweezer.

Authors:  Xin Li; Kuo Hao Lee; Spencer Shorkey; Jianhan Chen; Min Chen
Journal:  ACS Nano       Date:  2020-02-11       Impact factor: 15.881

5.  The pre-eminence of k(cat) in the manifestation of optimal enzymic activity delineated by using the Briggs-Haldane two-step irreversible kinetic model.

Authors:  K Brocklehurst; A Cornish-Bowden
Journal:  Biochem J       Date:  1976-10-01       Impact factor: 3.857

6.  Trends in global warming and evolution of matrix protein 2 family from influenza A virus.

Authors:  Shao-Min Yan; Guang Wu
Journal:  Interdiscip Sci       Date:  2009-11-14       Impact factor: 2.233

  6 in total

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