Barrier passage and protein dynamics in enzymatically catalyzed reactions.
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.
Antoniou
Dimitri
D
Department of Biophysics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Caratzoulas
Stavros
S
Kalyanaraman
C
C
Mincer
Joshua S
JS
Schwartz
Steven D
SD
D002384:Catalysis; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism*; D008956:Models, Chemical; D011487:Protein Conformation; D017510:Protein Folding; D014732:Vibration
D004798:Enzymes