Tunneling and coupled motion in the Escherichia coli dihydrofolate reductase catalysis - PubMed

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• PMID: 15080672
• DOI: 10.1021/ja031683w

Tunneling and coupled motion in the Escherichia coli dihydrofolate reductase catalysis

R Steven Sikorski et al. J Am Chem Soc. 2004.

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 degrees to 2 degrees coupled motion. The data also suggested environmentally coupled tunneling and commitment to catalysis on pre-steady-state isotope effects.

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