CATALYSIS IN INVERTED POTENTIAL-ENERGY PROFILES

被引:2
作者
EHRENBERG, M [1 ]
TAPIA, O [1 ]
机构
[1] UNIV UPPSALA, DEPT PHYS CHEM, S-75121 UPPSALA, SWEDEN
关键词
CATALYSIS; ENZYME MECHANISMS; BROWNIAN MOTION IN POTENTIAL WELLS; CHEMICAL REACTION RATE THEORY; CATALYTIC INACTIVATION;
D O I
10.1016/0301-4622(92)80030-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
When the activated state of a substrate molecule is chemically similar to the ground states of substrate or product, enzymes are limited in their ability to stabilize the activated state. In conventional schemes this leads to slow catalysis. We present a model, based on two postulates, that removes this limitation. Here catalysis is based on a vibrational excitation along the S --> P transition, that is isolated from other dynamic modes of the protein. We discuss testable (verifiable) predictions of the model.
引用
收藏
页码:157 / 167
页数:11
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