Page, Michael I. (1980) Transition states, standard states and enzymic catalysis. International Journal of Biochemistry, 11 (5). pp. 331-335. ISSN 1357-2725Metadata only available from this repository.
1. 1. Thermodynamic aspects of transition state theory are reviewed with particular reference to enzyme-catalysed reactions.
2. 2. Standard states must be specified when free energy changes of enzyme catalysed reactions are expressed graphically, otherwise false conclusions may be drawn.
3. 3. Enzymes cannot increase the rate of unimolecular reactions if either the transition state and ground state bind equally well to the enzyme or if the enzyme binds the ground state more tightly than the transition state. This is true even if the enzyme changes conformation during the reaction and even if the transition state is different in the presence and absence of enzyme.
|Subjects:||Q Science > Q Science (General)|
Q Science > QD Chemistry
|Schools:||School of Applied Sciences|
|Depositing User:||Sharon Beastall|
|Date Deposited:||12 Nov 2009 12:14|
|Last Modified:||12 Nov 2009 12:14|
Item control for Repository Staff only: