Barrier passage and protein dynamics in enzymatically catalyzed reactions

被引:112
作者
Antoniou, D
Caratzoulas, S
Kalyanaraman, C
Mincer, JS
Schwartz, SD
机构
[1] Albert Einstein Coll Med, Dept Biophys, Bronx, NY 10467 USA
[2] Albert Einstein Coll Med, Dept Biochem, Bronx, NY 10467 USA
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 2002年 / 269卷 / 13期
关键词
protein dynamics; enzyme catalysis; tunneling; promoting vibration; promoting mode;
D O I
10.1046/j.1432-1033.2002.03021.x
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
This review describes studies of particular enzymatically catalyzed reactions to investigate the possibility that catalysis is mediated by protein dynamics. That is, evolution has crafted the protein backbone of the enzyme to direct vibrations in such a fashion to speed reaction. The review presents the theoretical approach we have used to investigate this problem, but it is designed for the nonspecialist. The results show that in alcohol dehydrogenase, dynamic protein motion is in fact strongly coupled to chemical reaction in such a way as to promote catalysis. This result is in concert with both experimental data and interpretations for this and other enzyme systems studied in the laboratories of the two other investigators who have published reviews in this issue.
引用
收藏
页码:3103 / 3112
页数:10
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