About: Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions

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About: Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions Goto Sponge NotDistinct Permalink

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scientific article published on 01 January 1999

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rdf:type	Item
description	wetenschappelijk artikel (nl) наукова стаття, опублікована в січні 1999 (uk) articolo scientifico (pubblicato il 1999) (it) 1999 թվականին հրատարակված գիտական հոդված (hy) im Januar 1999 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en xineru de 1999 (ast) artikull shkencor i botuar më 01 janar 1999 (sq) scientific article published on 01 January 1999 (en)
publication date	wds:Q73043224-3AE39A8B-6EE5-400F-8953-C2969187405D
publication date	1999-01-01 00:00:00Z (xsd:dateTime)
cites work	wds:Q73043224-15E5700D-C318-4D7C-8D0C-39D6C27FAF49 wds:Q73043224-16C8C310-E763-48B0-97B9-1992D66C1CC0 wds:Q73043224-1C0E0927-2CBC-4A3C-A552-83C224F559B9 wds:Q73043224-32A3BEEF-14D4-48B2-9293-2179DC4D2376 wds:Q73043224-33C5C0AD-A91B-4438-BAD4-0080484216EF wds:Q73043224-3F8A7645-FC47-42AD-8ED9-E9F50D0D3830 wds:Q73043224-646EDF11-236C-443E-A60B-2CB85E7D804B wds:Q73043224-65779D05-58CA-486E-957A-280D8BADB5E8 wds:Q73043224-726CE55D-5FF2-4907-851B-6DAAAD914616 wds:Q73043224-830DE782-8C3D-4AB6-A511-20D8FC61D102 wds:Q73043224-84E497BE-8144-4060-8F70-5BE566F87BCB wds:Q73043224-8D584577-6788-44E6-9039-53E07C61309E wds:Q73043224-9543C1AD-185D-485D-8DF1-011DD8F200CF wds:Q73043224-9CE9D5B6-22C3-4412-B3DF-CF0953427372 wds:Q73043224-A008959B-05C0-44C8-A9CC-E9866E0A4801 wds:Q73043224-A2442EFC-20C3-43C0-AAAE-9A25A87D9750 wds:Q73043224-B77F0960-743C-4D39-9458-F02FECF6A9E8 wds:Q73043224-BBF73DF1-1C20-4A16-8ECB-7F4B1C82C993 wds:Q73043224-C030467A-50A6-4CFD-ABD4-33435CE31452 wds:Q73043224-C87B77D8-3BBE-419C-AA78-129028171811 wds:Q73043224-CAE72955-B05E-4EBD-957B-D4CAB5590F62 wds:Q73043224-CF9846F3-DED0-419E-BB9F-D00067259BE6 wds:Q73043224-D3C4C4B2-B9AF-41FF-A04E-0E95D7A38C49 wds:Q73043224-DEF67B29-52F8-40E5-A493-84CC10259B82 wds:Q73043224-E13236BB-4886-4F38-84AA-CC0BDE57A17A wds:Q73043224-E8E12103-2A7F-4959-B0D2-5C61ACEFEE84 wds:Q73043224-E9F87A35-54F6-405F-938D-2CB2D557D99C wds:Q73043224-EB9B9A2A-CEC6-4B11-889B-78707A795E02 wds:Q73043224-F73291A2-FCB0-4220-B9C8-3FAEEAA04BF1
cites work	The carbonic anhydrases: widening perspectives on their evolution, expression and function On the Theory of Oxidation‐Reduction Reactions Involving Electron Transfer. I Refined structure of human carbonic anhydrase II at 2.0 A resolution Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes The Catalytic Mechanism of Carbonic Anhydrase. Hydrogen-Isotope Effects on the Kinetic Parameters of the Human C Isoenzyme Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water Refined structure of bovine carbonic anhydrase III at 2.0 A resolution Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III Disruption of the active site solvent network in carbonic anhydrase II decreases the efficiency of proton transfer. 35 Carbonic anhydrase: Oxygen-18 exchange catalyzed by an enzyme with rate-contributing Proton-transfer steps A Correlation of Reaction Rates Parameters for the Description of Transition States Chemical and Electrochemical Electron-Transfer Theory Physical organic chemistry of benzisoxazoles. II. Linearity of the Broensted free energy relation for the base-catalyzed decomposition of benzisoxazoles A primer for the Bema Hapothle. An empirical approach to the characterization of changing transition-state structures Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters Evaluation of the internal equilibrium constant for 3-oxo-delta 5-steroid isomerase using the D38E and D38N mutants: the energetic basis for catalysis Influence of amino acid replacement at position 198 on catalytic properties of zinc-bound water in human carbonic anhydrase III X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesis Proton transfer by histidine 67 in site-directed mutants of human carbonic anhydrase III. Proton transfer in the catalytic mechanism of carbonic anhydrase. Effects of placing histidine residues at various positions in the active site of human isoenzyme II An experimentally based family of potential energy surfaces for hydride transfer between NAD+ analogs The Magnitude of the Primary Kinetic Isotope Effect for Compounds of Hydrogen and Deuterium Interaction and influence of phenylalanine-198 and threonine-199 on catalysis by human carbonic anhydrase III Carbon dioxide hydration activity of carbonic anhydrase in mixtures of water and deuterium oxide The interaction of sulfate with carbonic anhydrase A study of the histidine residues of human carbonic anhydrase C using 270 MHz proton magnetic resonance
author name string	wds:Q73043224-4ECE659F-AB4C-4F58-BD4B-F3250B0F5EC5 wds:Q73043224-A235F12D-91D3-4D2F-AE6D-6D8F5AD96769
author name string	D N Silverman A J Kresge
rdfs:label	Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (en) Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (nl) Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (sq)
skos:prefLabel	Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (en) Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (nl) Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (sq)
name	Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (en) Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (nl) Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (sq)
title	wds:Q73043224-4E49B99C-B3F4-42E3-B63B-83FAEAFE44C0
title	Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (en)
page(s)	wds:Q73043224-5FB5CA5F-AF88-4E0B-A9A8-A019BA3A05D3
page(s)	276-297
instance of	wds:Q73043224-EAE1F323-5071-4FD4-AD27-4FBF6D4CB8C3
instance of	scholarly article
PubMed ID	wds:Q73043224-A8EF2731-0A91-4721-A555-E87AD5E40CCC
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/10507009
PubMed ID	10507009
published in	wds:Q73043224-971C0A86-0C6B-4C00-8B8F-8E6F3AA9F584
published in	Methods in Enzymology
volume	wds:Q73043224-6F8C4172-F9A8-4117-8B6C-EA222CCCBA20
volume	308
DOI	wds:Q73043224-314BF6FF-3B98-45EA-93B3-08319D458B8F
DOI	http://dx.doi.org/10.1016/S0076-6879(99)08014-3
DOI	10.1016/S0076-6879(99)08014-3
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q73043224
is cites work of	Multidimensional tunneling, recrossing, and the transmission coefficient for enzymatic reactions

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