Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
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Methods to Increase the Metabolic Stability of (18)F-RadiotracersEffects of Cavities at the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase on Structure, Dynamics and CatalysisQuantum Tunnelling to the Origin and Evolution of LifeKinetic isotope effects as a probe of hydrogen transfers to and from common enzymatic cofactorsExtension and limits of the network of coupled motions correlated to hydride transfer in dihydrofolate reductase.Concerted versus stepwise mechanism in thymidylate synthase.Preserved hydride transfer mechanism in evolutionarily divergent thymidylate synthases.Role of long-range protein dynamics in different thymidylate synthase catalyzed reactions.Network of remote and local protein dynamics in dihydrofolate reductase catalysisStereospecific multiple isotopic labeling of benzyl alcohol.Activation of Two Sequential H-transfers in the Thymidylate Synthase Catalyzed Reaction.Examinations of the Chemical Step in Enzyme Catalysis.A critical test of the "tunneling and coupled motion" concept in enzymatic alcohol oxidation.The general base in the thymidylate synthase catalyzed proton abstraction.Substrate and Transition State Binding in Alkaline Phosphatase Analyzed by Computation of Oxygen Isotope Effects.Free-Energy Landscape and Proton Transfer Pathways in Oxidative Deamination by Methylamine Dehydrogenase.Wide-dynamic-range kinetic investigations of deep proton tunnelling in proteins.Deuterium- and Tritium-Labelled Compounds: Applications in the Life Sciences.Change in heat capacity accurately predicts vibrational coupling in enzyme catalyzed reactions.Possible interstellar formation of glycine through a concerted mechanism: a computational study on the reaction of CH2[double bond, length as m-dash]NH, CO2 and H2.Protein motions and dynamic effects in enzyme catalysis.Mechanism-Informed Refinement Reveals Altered Substrate-Binding Mode for Catalytically Competent Nitroreductase.Bacterial versus human thymidylate synthase: Kinetics and functionality.
P2860
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P2860
Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
description
2013 nî lūn-bûn
@nan
2013 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2013年の論文
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2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
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name
Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
@ast
Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
@en
type
label
Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
@ast
Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
@en
prefLabel
Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
@ast
Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
@en
P2093
P2860
P1433
P1476
Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.
@en
P2093
Amnon Kohen
Daniel Roston
Zahidul Islam
P2860
P304
P356
10.3390/MOLECULES18055543
P407
P577
2013-05-14T00:00:00Z