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Communication

Tunneling and Coupled Motion in the Escherichia coli Dihydrofolate Reductase Catalysis

Supporting Info

R. Steven Sikorski,^† Lin Wang,^† Kelli A. Markham,^† P. T. Ravi Rajagopalan,^‡ Stephen J. Benkovic,^‡ and Amnon Kohen*^†

Department of Chemistry, University of Iowa, Iowa City, Iowa 52242, and Department of Chemistry, Pennsylvania State University, University Park, Pennsylvania 16802

J. Am. Chem. Soc., 2004, 126 (15), pp 4778–4779

DOI: 10.1021/ja031683w

Publication Date (Web): March 26, 2004

†

University of Iowa.

‡

Pennsylvania State University.

In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

amnon-kohen@uiowa.edu

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.

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