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

来源：

BIOPHYSICAL CHEMISTRY | 1992年 / 43卷 / 02期

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

页码：157 / 167

页数：11

共 45 条

[1] UNUSUAL VALYL-TRANSFER RIBONUCLEIC-ACID SYNTHETASE MUTANT OF ESCHERICHIA-COLI [J].

ANDERSON, JJ ;

NEIDHARD.FC .

JOURNAL OF BACTERIOLOGY, 1972, 109 (01) :307-&

[2] GROWTH-LINKED INSTABILITY OF A MUTANT VALYL-TRANSFER RIBONUCLEIC-ACID SYNTHETASE IN ESCHERICHIA-COLI [J].

ANDERSON, JJ ;

NEIDHARD.FC .

JOURNAL OF BACTERIOLOGY, 1972, 109 (01) :315-&

[3]

[Anonymous], 1946, CHEM ENG NEWS, DOI DOI 10.1021/CEN-V024N010.P1375

[4]

[Anonymous], 1978, TRANSITION STATES BI

[5] SOLVENT VISCOSITY AND PROTEIN DYNAMICS [J].

BEECE, D ;

EISENSTEIN, L ;

FRAUENFELDER, H ;

GOOD, D ;

MARDEN, MC ;

REINISCH, L ;

REYNOLDS, AH ;

SORENSEN, LB ;

YUE, KT .

BIOCHEMISTRY, 1980, 19 (23) :5147-5157

[6] PROTEIN DYNAMICS AND REACTION-RATES - MODE-SPECIFIC CHEMISTRY IN LARGE MOLECULES [J].

BIALEK, W ;

ONUCHIC, JN .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (16) :5908-5912

[7]

BRUTLAG D, 1972, J BIOL CHEM, V247, P241

[8] SLOW INACTIVATION OF RIBULOSEBISPHOSPHATE CARBOXYLASE DURING CATALYSIS IS NOT DUE TO DECARBAMYLATION OF THE CATALYTIC SITE [J].

EDMONDSON, DL ;

BADGER, MR ;

ANDREWS, TJ .

PLANT PHYSIOLOGY, 1990, 93 (04) :1383-1389

[9] SUBSTRATE ISOMERIZATION INHIBITS RIBULOSEBISPHOSPATE CARBOXYLASE-OXYGENASE DURING CATALYSIS [J].

EDMONDSON, DL ;

KANE, HJ ;

ANDREWS, TJ .

FEBS LETTERS, 1990, 260 (01) :62-66

[10] A KINETIC CHARACTERIZATION OF SLOW INACTIVATION OF RIBULOSEBISPHOSPHATE CARBOXYLASE DURING CATALYSIS [J].

EDMONDSON, DL ;

BADGER, MR ;

ANDREWS, TJ .

PLANT PHYSIOLOGY, 1990, 93 (04) :1376-1382

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