A link between protein structure and enzyme catalyzed hydrogen tunneling
about
Enzymes: An integrated view of structure, dynamics and functionCrystal structure of the monomeric isocitrate dehydrogenase in the presence of NADP+: insight into the cofactor recognition, catalysis, and evolutionEnzyme structure and dynamics affect hydrogen tunneling: The impact of a remote side chain (I553) in soybean lipoxygenase-1Origins of the high catalytic activity of human alcohol dehydrogenase 4 studied with horse liver A317C alcohol dehydrogenaseAtomic-Resolution Structures of Horse Liver Alcohol Dehydrogenase with NAD + and Fluoroalcohols Define Strained Michaelis ComplexesEffects of Cavities at the Nicotinamide Binding Site of Liver Alcohol Dehydrogenase on Structure, Dynamics and CatalysisAt the dawn of the 21st century: Is dynamics the missing link for understanding enzyme catalysis?A novel subtype of class II alcohol dehydrogenase in rodents. Unique Pro(47) and Ser(182) modulates hydride transfer in the mouse enzymeEffects of the donor-acceptor distance and dynamics on hydride tunneling in the dihydrofolate reductase catalyzed reactionPerspective: Defining and quantifying the role of dynamics in enzyme catalysisLinking protein structure and dynamics to catalysis: the role of hydrogen tunnelling.The role of enzyme dynamics and tunnelling in catalysing hydride transfer: studies of distal mutants of dihydrofolate reductase.Effects of a distal mutation on active site chemistry.Structural and Kinetic Studies of Formate Dehydrogenase from Candida boidinii.Accurate metal-site structures in proteins obtained by combining experimental data and quantum chemistry.An integrated model for enzyme catalysis emerges from studies of hydrogen tunneling.Update 1 of: Tunneling and dynamics in enzymatic hydride transfer.Natural engineering principles of electron tunnelling in biological oxidation-reduction.Importance of protein dynamics during enzymatic C-H bond cleavage catalysis.Examining the case for the effect of barrier compression on tunneling, vibrationally enhanced catalysis, catalytic entropy and related issuesTen-nanosecond molecular dynamics simulation of the motions of the horse liver alcohol dehydrogenase.PhCH2O- complex.Barrier passage and protein dynamics in enzymatically catalyzed reactions.Isotope effects as probes for enzyme catalyzed hydrogen-transfer reactions.Multidimensional tunneling, recrossing, and the transmission coefficient for enzymatic reactionsAnalysis of Hydrogen Tunneling in an Enzyme Active Site using von Neumann MeasurementsActive site hydrophobic residues impact hydrogen tunneling differently in a thermophilic alcohol dehydrogenase at optimal versus nonoptimal temperatures.Gauging the flexibility of the active site in soybean lipoxygenase-1 (SLO-1) through an atom-centered density matrix propagation (ADMP) treatment that facilitates the sampling of rare events.Anticorrelated motions as a driving force in enzyme catalysis: the dehydrogenase reaction.Kinetic isotope effects as a probe of hydrogen transfers to and from common enzymatic cofactorsHydrogen tunneling in enzymes and biomimetic models.Protein dynamics and the enzymatic reaction coordinate.Protein motions and the activation of the CH bond catalyzed by dihydrofolate reductase.Enzymatic methyl transfer: role of an active site residue in generating active site compaction that correlates with catalytic efficiency.An analysis of reaction pathways for proton tunnelling in methylamine dehydrogenaseThe ternary complex of Pseudomonas aeruginosa alcohol dehydrogenase with NADH and ethylene glycolThe effect of active-site isoleucine to alanine mutation on the DHFR catalyzed hydride-transfer.An Analysis of All the Relevant Facts and Arguments Indicates that Enzyme Catalysis Does Not Involve Large Contributions from Nuclear Tunneling.Investigating inner-sphere reorganization via secondary kinetic isotope effects in the C-H cleavage reaction catalyzed by soybean lipoxygenase: tunneling in the substrate backbone as well as the transferred hydrogen.Deuterium isotope effects during carbon-hydrogen bond cleavage by trimethylamine dehydrogenase. Implications for mechanism and vibrationally assisted hydrogen tunneling in wild-type and mutant enzymes.H-tunneling in the multiple H-transfers of the catalytic cycle of morphinone reductase and in the reductive half-reaction of the homologous pentaerythritol tetranitrate reductase.
P2860
Q25255883-815AF765-EB9F-4544-83C0-D5A3AAD073B6Q27641663-BFDD00F9-B2A8-4703-8C4C-DBCBAF40A25FQ27649699-D145E913-FD5C-4B3A-9D16-06944A49C09AQ27666387-E4911F82-9625-4069-A258-DB2708B653EFQ27678715-F1B03BC0-43FB-43A8-BC06-774BBBC4A5C2Q27681376-876BA445-E9D1-4C0F-BDCA-1354BF181C1DQ28271287-742686BE-A3E9-4046-9114-4789E50646DEQ28508032-88497869-D384-43E5-B7E7-368B567666CFQ28649378-C40780F2-25BF-4899-B613-38E0CD01C2E8Q28834243-A23DC5C4-7BAB-4DB8-B774-0D56BA418E41Q30355965-0712295F-7367-4D78-B2F9-700D758A4B8CQ30478319-FD2D920E-427A-4AC0-9913-1D1553C35AC1Q30483738-684C1F4F-DD5F-43A5-AA98-70829F774479Q30775729-4203B3A7-4C43-4418-A8F8-56B59D6D94E7Q33271330-5B2C5E7A-86A8-441E-A8DA-F103FA89323FQ33758599-DB51F077-209E-4A0E-BE8B-FF980116049EQ33794709-7CECB8E8-7CEA-4557-8BFF-97FEB41336D7Q33881476-37B70F3A-17A2-4776-BD4A-323EC5FEFD70Q33881988-1F389327-DBC4-4F05-9407-5609D2FC1789Q33917537-7E282C6F-1B40-4ECF-B802-15179787B7D7Q34429171-7C6F6A96-01B7-4C49-B734-F406F1817F57Q34707033-AD2F21D6-37BB-4CDB-89E3-ABA7E01BC578Q35127653-6999B321-657B-4BA1-B5A2-81E355126961Q35774258-324F76FC-1FA7-44AD-810A-519931A2E768Q36190548-FADA68FE-E7B5-42CC-8DA1-29CE46E7C328Q36401744-8334CD84-12C6-44D7-8693-06BD89D55782Q36572667-8464D068-2E61-4BF2-AEF6-E16DD2E27075Q37513201-C7DA246C-F868-457D-83AB-7E79103D5057Q37624546-BFC3AF31-C1E3-4CBC-AD9C-6D68856F0A6AQ37695037-339E258C-8B22-483E-BD46-706E34C3FE14Q38091003-6F2739A2-163F-41CE-B71D-3843DA849757Q38205312-A10F4ECF-1CF6-4A1F-B1FF-122A6EC135E1Q39202928-193C5F76-F0CE-448E-9B15-15E9065627D5Q39482505-EEF80444-0F3A-4512-B40A-2ED06B9E7A2EQ42006163-92E39DDB-6601-4A67-A71A-57117EF1F4BAQ42122813-12F56D70-684F-4810-AA6D-205678BFA406Q42132462-26530AF0-ADCA-481F-A97D-FBDE4DDADAC0Q42140470-910B0737-6D4C-457E-BE4B-0CF703912445Q43576565-1C3A83C3-8075-4C22-A0B4-447209C7F273Q44564228-80CF2C99-2FA5-4CA4-AD26-E33B677255FC
P2860
A link between protein structure and enzyme catalyzed hydrogen tunneling
description
1997 nî lūn-bûn
@nan
1997 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
A link between protein structure and enzyme catalyzed hydrogen tunneling
@ast
A link between protein structure and enzyme catalyzed hydrogen tunneling
@en
A link between protein structure and enzyme catalyzed hydrogen tunneling
@nl
type
label
A link between protein structure and enzyme catalyzed hydrogen tunneling
@ast
A link between protein structure and enzyme catalyzed hydrogen tunneling
@en
A link between protein structure and enzyme catalyzed hydrogen tunneling
@nl
prefLabel
A link between protein structure and enzyme catalyzed hydrogen tunneling
@ast
A link between protein structure and enzyme catalyzed hydrogen tunneling
@en
A link between protein structure and enzyme catalyzed hydrogen tunneling
@nl
P2093
P2860
P356
P1476
A link between protein structure and enzyme catalyzed hydrogen tunneling
@en
P2093
B J Bahnson
B M Goldstein
J P Klinman
P2860
P304
P356
10.1073/PNAS.94.24.12797
P407
P577
1997-11-25T00:00:00Z