Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis

R. Steven Sikorski; Lin Wang; Kelli A. Markham; P. T.Ravi Rajagopalan; Stephen J. Benkovic; Amnon Kohen

doi:10.1021/ja031683w

Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis

R. Steven Sikorski, Lin Wang, Kelli A. Markham, P. T.Ravi Rajagopalan, Stephen J. Benkovic, Amnon Kohen

Chemistry

Research output: Contribution to journal › Article › peer-review

181 Scopus citations

Abstract

H-transfer was studied in the complex kinetic cascade of dihydrofolate reductase. Intrinsic kinetic isotope effects, their temperature dependence, and other temperature-dependent parameters indicated H-tunneling, but no 1° to 2° coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.

Original language	English (US)
Pages (from-to)	4778-4779
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	126
Issue number	15
DOIs	https://doi.org/10.1021/ja031683w
State	Published - Apr 21 2004

All Science Journal Classification (ASJC) codes

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja031683w

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abstract = "H-transfer was studied in the complex kinetic cascade of dihydrofolate reductase. Intrinsic kinetic isotope effects, their temperature dependence, and other temperature-dependent parameters indicated H-tunneling, but no 1° to 2° coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.",

author = "Sikorski, {R. Steven} and Lin Wang and Markham, {Kelli A.} and Rajagopalan, {P. T.Ravi} and Benkovic, {Stephen J.} and Amnon Kohen",

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AU - Sikorski, R. Steven

AU - Wang, Lin

AU - Markham, Kelli A.

AU - Rajagopalan, P. T.Ravi

AU - Benkovic, Stephen J.

AU - Kohen, Amnon

PY - 2004/4/21

Y1 - 2004/4/21

N2 - H-transfer was studied in the complex kinetic cascade of dihydrofolate reductase. Intrinsic kinetic isotope effects, their temperature dependence, and other temperature-dependent parameters indicated H-tunneling, but no 1° to 2° coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.

AB - H-transfer was studied in the complex kinetic cascade of dihydrofolate reductase. Intrinsic kinetic isotope effects, their temperature dependence, and other temperature-dependent parameters indicated H-tunneling, but no 1° to 2° coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.

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Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis

Abstract

All Science Journal Classification (ASJC) codes

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