Catalytic Power and Transition-State Stabilization
This book is about the use of the transition-state concept, and of ideas about transition-state structure and the stabilization of transition states in catalysis, in understanding the rate processes of biochemistry. Essentially all the reactions considered are enzyme-catalyzed reactions or reactions studied in order to illuminate enzyme catalysis. In view of our thesis in this volume—that the transition state and its structure and interactions are the central feature of catalysis it is interesting to note that in much of the current writing on enzyme catalysis, the transition state is mentioned rather more rarely than might have been anticipated and its stabilization is sometimes relegated to the position of a single item in a long list of potential contributions to catalytic power. This is true in the pioneering volumes of Bruice and Benkovic,(1) in the monographs of Jencks(2) and Bender,(3) and in the recent reviews of Jencks(4) and Bruice.(5) It is likewise true of many other valuable books and articles, of which well over 5000 are cited in the sources just mentioned. Obvious exceptions to this custom are, of course, the authors interested in transition-state analogs, such as Lienhardt(6) and Wolfenden,t(7) but the general tendency is clear. There is certainly no agreement that all we need to know in order to understand enzyme catalysis is the structure of the transition state and the manner in which it is stabilized.
KeywordsFree Energy Transition State Standard Reaction Catalytic Power Apparent Free Energy
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