Impact of Protein Flexibility on Hydride-Transfer Parameters in Thermophilic and Psychrophilic Alcohol Dehydrogenases
- 20 July 2004
- journal article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 126 (31) , 9500-9501
- https://doi.org/10.1021/ja047087z
Abstract
The hydride transfer catalyzed by thermophilic alcohol dehydrogenase (htADH) exhibits sharply different kinetic and activation parameters from that catalyzed by the more flexible psychrophilic alcohol dehydrogenase (psADH). In addition, the hydride transfer in htADH is affected by mutating two distal residues that are suggested to be responsible for the decreased local protein flexibility in htADH. These observations provide support for the view that protein dynamics is tightly coupled to the hydrogen-transfer processes in these enzymes.Keywords
This publication has 10 references indexed in Scilit:
- Proton-Coupled Electron Transfer in Soybean LipoxygenaseJournal of the American Chemical Society, 2004
- Crystal Structure and Amide H/D Exchange of Binary Complexes of Alcohol Dehydrogenase from Bacillus stearothermophilus: Insight into Thermostability and Cofactor Binding,Biochemistry, 2004
- A Perspective on Enzyme CatalysisScience, 2003
- Temperature-Dependent Isotope Effects in Soybean Lipoxygenase-1: Correlating Hydrogen Tunneling with Protein DynamicsJournal of the American Chemical Society, 2002
- Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibilityPublished by Elsevier ,2000
- Protein Flexibility Correlates with Degree of Hydrogen Tunneling in Thermophilic and Mesophilic Alcohol DehydrogenasesJournal of the American Chemical Society, 2000
- Enzyme dynamics and hydrogen tunnelling in a thermophilic alcohol dehydrogenaseNature, 1999
- Enzyme Catalysis: Beyond Classical ParadigmsAccounts of Chemical Research, 1998
- A link between protein structure and enzyme catalyzed hydrogen tunnelingProceedings of the National Academy of Sciences, 1997
- Purification and characterization of the alcohol dehydrogenase from a novel strain of Bacillus stearothermophilus growing at 70°CThe International Journal of Biochemistry & Cell Biology, 1996