Although many aspects of enzyme catalysis have been constructively analyzed, 1-52 there are still many aspects that are imperfectly understood. Of particular interest in this regard are …
We present an atomic-level description of the reaction chemistry of an enzyme-catalyzed reaction dominated by proton tunneling. By solving structures of reaction intermediates at …
ZD Nagel, JP Klinman - Chemical reviews, 2010 - ncbi.nlm.nih.gov
Enzymes continue to be the subject of intensive research efforts because of their ability to accelerate chemical reactions by factors as large as 1020 with extraordinary selectivity. 1 …
J Pu, S Ma, J Gao, DG Truhlar - The Journal of Physical Chemistry …, 2005 - ACS Publications
The H/D primary kinetic isotope effect (KIE) for the hydride transfer reaction catalyzed by Escherichia coli dihydrofolate reductase (ec DHFR) is calculated as a function of …
JD McGeagh, KE Ranaghan, AJ Mulholland - Biochimica et Biophysica …, 2011 - Elsevier
The role of protein dynamics in enzyme catalysis is one of the most active and controversial areas in enzymology today. Some researchers claim that protein dynamics are at the heart …
ZX Liang, JP Klinman - Current opinion in structural biology, 2004 - Elsevier
Accumulating experimental evidence suggests that the occurrence of hydrogen tunneling is likely to be widespread in enzyme-catalyzed reactions. The realization that hydrogen can …
Kinetic isotope effects (KIEs) and their temperature dependence can probe the structural and dynamic nature of enzyme-catalyzed proton or hydride transfers. The molecular …
Covering: 1980–September 2004 The mechanism of amine oxidation by flavoprotein enzymes is critically analysed through analysis of available experimental data. The review …
Use of the pressure dependence of kinetic isotope effects, coupled with a study of their temperature dependence, as a probe for promoting motions in enzymatic hydrogen …