Evidence that a ‘dynamic knockout’ in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis
出版年份 2012 全文链接
标题
Evidence that a ‘dynamic knockout’ in Escherichia coli dihydrofolate reductase does not affect the chemical step of catalysis
作者
关键词
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出版物
Nature Chemistry
Volume 4, Issue 4, Pages 292-297
出版商
Springer Nature
发表日期
2012-03-09
DOI
10.1038/nchem.1296
参考文献
相关参考文献
注意:仅列出部分参考文献,下载原文获取全部文献信息。- Effect of pH on Hydride Transfer by Escherichia coli Dihydrofolate Reductase
- (2011) E. Joel Loveridge et al. CHEMBIOCHEM
- The Role of Large-Scale Motions in Catalysis by Dihydrofolate Reductase
- (2011) E. Joel Loveridge et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Catalysis by dihydrofolate reductase and other enzymes arises from electrostatic preorganization, not conformational motions
- (2011) A. J. Adamczyk et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis
- (2011) G. Bhabha et al. SCIENCE
- The Temperature Dependence of the Kinetic Isotope Effects of Dihydrofolate Reductase fromThermotoga maritimaIs Influenced by Intersubunit Interactions
- (2010) E. Joel Loveridge et al. BIOCHEMISTRY
- Protein dynamics and enzyme catalysis: Insights from simulations
- (2010) John D. McGeagh et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- Slow Conformational Motions That Favor Sub-picosecond Motions Important for Catalysis
- (2010) J. R. Exequiel T. Pineda et al. JOURNAL OF PHYSICAL CHEMISTRY B
- An analysis of all the relevant facts and arguments indicates that enzyme catalysis does not involve large contributions from nuclear tunneling
- (2010) Shina C. L. Kamerlin et al. JOURNAL OF PHYSICAL ORGANIC CHEMISTRY
- Heavy atom motions and tunneling in hydrogen transfer reactions: the importance of the pre-tunneling state
- (2010) Hans-Heinrich Limbach et al. JOURNAL OF PHYSICAL ORGANIC CHEMISTRY
- Solvent Effects on Catalysis byEscherichia coliDihydrofolate Reductase
- (2010) E. Joel Loveridge et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Probing coupled motions in enzymatic hydrogen tunnelling reactions
- (2009) Rudolf K. Allemann et al. BIOCHEMICAL SOCIETY TRANSACTIONS
- Structural and mechanistic aspects of flavoproteins: probes of hydrogen tunnelling
- (2009) Sam Hay et al. FEBS Journal
- Evidence To Support the Hypothesis That Promoting Vibrations Enhance the Rate of an Enzyme Catalyzed H-Tunneling Reaction
- (2009) Christopher R Pudney et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Functionally Important Conformations of the Met20 Loop in Dihydrofolate Reductase are Populated by Rapid Thermal Fluctuations
- (2009) Karunesh Arora et al. JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
- Enzymatic transition states and dynamic motion in barrier crossing
- (2009) Steven D Schwartz et al. Nature Chemical Biology
- A 21st century revisionist's view at a turning point in enzymology
- (2009) Zachary D Nagel et al. Nature Chemical Biology
- Enzyme millisecond conformational dynamics do not catalyze the chemical step
- (2009) A. V. Pisliakov et al. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
- Solvent Effects on Environmentally Coupled Hydrogen Tunnelling During Catalysis by Dihydrofolate Reductase from Thermotoga maritima
- (2008) E. Joel Loveridge et al. CHEMISTRY-A EUROPEAN JOURNAL
- Nuclear Quantum Tunneling in the Light-activated Enzyme Protochlorophyllide Oxidoreductase
- (2008) Derren J. Heyes et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Hydrogen Tunneling in Glucose Oxidation by the ArchaeonThermoplasma acidophilum
- (2008) Kandiah Anandarajah et al. ZEITSCHRIFT FUR PHYSIKALISCHE CHEMIE-INTERNATIONAL JOURNAL OF RESEARCH IN PHYSICAL CHEMISTRY & CHEMICAL PHYSICS
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