Importance of Barrier Shape in Enzyme-catalyzed Reactions
Open Access
- 1 March 2001
- journal article
- Published by Elsevier BV
- Vol. 276 (9), 6234-6242
- https://doi.org/10.1074/jbc.m008141200
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- α-Secondary Tritium Kinetic Isotope Effects Indicate Hydrogen Tunneling and Coupled Motion Occur in the Oxidation of l-Malate by NAD-Malic EnzymeBiochemistry, 1999
- Enzymatic H-Transfer Requires Vibration-Driven Extreme TunnelingBiochemistry, 1999
- Proton and hydrogen atom tunnelling in hydrolytic and redox enzyme catalysisCanadian Journal of Chemistry, 1999
- Large Kinetic Isotope Effects in Methane Oxidation Catalyzed by Methane Monooxygenase: Evidence for C−H Bond Cleavage in a Reaction Cycle IntermediateBiochemistry, 1996
- Electron Transfer Reactions between Aromatic Amine Dehydrogenase and AzurinBiochemistry, 1995
- Unusually large isotope effect for the reaction of aromatic amine dehydrogenase. A common feature of quinoproteins?Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- Hydrogen tunneling in the flavoenzyme monoamine oxidase BBiochemistry, 1994
- Structure of an Electron Transfer Complex: Methylamine Dehydrogenase, Amicyanin, and Cytochrome c 551iScience, 1994
- Purification of ras farnesyl:Protein transferaseMethods, 1990
- Brownian motion in a field of force and the diffusion model of chemical reactionsPhysica, 1940