(Q73043224)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10507009%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

title

Application of Marcus rate theory to proton transfer in enzyme-catalyzed reactions (English)

1 reference

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31 October 2019

author name string

A J Kresge

series ordinal

1

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31 October 2019

D N Silverman

series ordinal

2

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31 October 2019

publication date

1 January 1999

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31 October 2019

published in

Methods in Enzymology

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31 October 2019

volume

308

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31 October 2019

page(s)

276-297

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On the Theory of Oxidation‐Reduction Reactions Involving Electron Transfer. I

31 October 2019

cites work

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Parameters for the Description of Transition States

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A Correlation of Reaction Rates

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A primer for the Bema Hapothle. An empirical approach to the characterization of changing transition-state structures

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Physical organic chemistry of benzisoxazoles. II. Linearity of the Broensted free energy relation for the base-catalyzed decomposition of benzisoxazoles

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The Magnitude of the Primary Kinetic Isotope Effect for Compounds of Hydrogen and Deuterium

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7 January 2021

Understanding the rates of certain enzyme-catalyzed reactions: proton abstraction from carbon acids, acyl-transfer reactions, and displacement reactions of phosphodiesters

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Evaluation of the internal equilibrium constant for 3-oxo-delta 5-steroid isomerase using the D38E and D38N mutants: the energetic basis for catalysis

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The catalytic mechanism of carbonic anhydrase: implications of a rate-limiting protolysis of water

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The Catalytic Mechanism of Carbonic Anhydrase. Hydrogen-Isotope Effects on the Kinetic Parameters of the Human C Isoenzyme

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7 January 2021

Role of histidine 64 in the catalytic mechanism of human carbonic anhydrase II studied with a site-specific mutant

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7 January 2021

Refined structure of human carbonic anhydrase II at 2.0 A resolution

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7 January 2021

Structure of native and apo carbonic anhydrase II and structure of some of its anion-ligand complexes

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Carbon dioxide hydration activity of carbonic anhydrase in mixtures of water and deuterium oxide

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7 January 2021

Disruption of the active site solvent network in carbonic anhydrase II decreases the efficiency of proton transfer.

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X-ray crystallographic studies of alanine-65 variants of carbonic anhydrase II reveal the structural basis of compromised proton transfer in catalysis

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7 January 2021

The carbonic anhydrases: widening perspectives on their evolution, expression and function

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Refined structure of bovine carbonic anhydrase III at 2.0 A resolution

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7 January 2021

Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesis

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Influence of amino acid replacement at position 198 on catalytic properties of zinc-bound water in human carbonic anhydrase III

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7 January 2021

Interaction and influence of phenylalanine-198 and threonine-199 on catalysis by human carbonic anhydrase III

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7 January 2021

Proton transfer by histidine 67 in site-directed mutants of human carbonic anhydrase III.

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7 January 2021

35 Carbonic anhydrase: Oxygen-18 exchange catalyzed by an enzyme with rate-contributing Proton-transfer steps

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7 January 2021

The interaction of sulfate with carbonic anhydrase

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7 January 2021

Rate-equilibria relationships in intramolecular proton transfer in human carbonic anhydrase III

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7 January 2021

A study of the histidine residues of human carbonic anhydrase C using 270 MHz proton magnetic resonance

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7 January 2021

An experimentally based family of potential energy surfaces for hydride transfer between NAD+ analogs

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7 January 2021

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

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7 January 2021

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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10507009%20AND%20SRC:MED&resulttype=core&format=json

31 October 2019

1 reference