Barrier passage and protein dynamics in enzymatically catalyzed reactions

Dimitri Antoniou; Stavros Caratzoulas; C. Kalyanaraman; Joshuas S. Mincer; Steven D. Schwartz

doi:10.1046/j.1432-1033.2002.03021.x

Barrier passage and protein dynamics in enzymatically catalyzed reactions

Dimitri Antoniou, Stavros Caratzoulas, C. Kalyanaraman, Joshuas S. Mincer, Steven D. Schwartz

Research output: Contribution to journal › Short survey › peer-review

125 Scopus citations

Abstract

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.

Original language	English (US)
Pages (from-to)	3103-3112
Number of pages	10
Journal	European Journal of Biochemistry
Volume	269
Issue number	13
DOIs	https://doi.org/10.1046/j.1432-1033.2002.03021.x
State	Published - 2002

Keywords

Enzyme catalysis
Promoting mode
Promoting vibration
Protein dynamics
Tunneling

ASJC Scopus subject areas

Biochemistry

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10.1046/j.1432-1033.2002.03021.x

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title = "Barrier passage and protein dynamics in enzymatically catalyzed reactions",

abstract = "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.",

keywords = "Enzyme catalysis, Promoting mode, Promoting vibration, Protein dynamics, Tunneling",

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journal = "European Journal of Biochemistry",

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T1 - Barrier passage and protein dynamics in enzymatically catalyzed reactions

AU - Antoniou, Dimitri

AU - Caratzoulas, Stavros

AU - Kalyanaraman, C.

AU - Mincer, Joshuas S.

AU - Schwartz, Steven D.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

KW - Enzyme catalysis

KW - Promoting mode

KW - Promoting vibration

KW - Protein dynamics

KW - Tunneling

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U2 - 10.1046/j.1432-1033.2002.03021.x

DO - 10.1046/j.1432-1033.2002.03021.x

M3 - Short survey

C2 - 12084050

SN - 0014-2956

VL - 269

SP - 3103

EP - 3112

JO - European Journal of Biochemistry

JF - European Journal of Biochemistry

IS - 13

ER -

Barrier passage and protein dynamics in enzymatically catalyzed reactions

Abstract

Keywords

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