pH Dependence of deuterium isotope effects and tritium exchange in the bovine plasma amine oxidase reaction: a role for single-base catalysis in amine oxidation and imine exchange

Biochemistry ◽  
1986 ◽  
Vol 25 (8) ◽  
pp. 1898-1904 ◽  
Author(s):  
Martin Farnum ◽  
Monica Palcic ◽  
Judith Pollock Klinman
Keyword(s):  
Amine Oxidase ◽  
Isotope Effects ◽  
Ph Dependence ◽  
Base Catalysis ◽  
Single Base ◽  
Amine Oxidation ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase ◽  
Deuterium Isotope Effects ◽  
Oxidase Reaction

Isotopic probes yield microscopic constants: separation of binding energy from catalytic efficiency in the bovine plasma amine oxidase reaction

Biochemistry ◽  
1983 ◽  
Vol 22 (25) ◽  
pp. 5957-5966 ◽  
Author(s):  
Monica M. Palcic ◽  
Judith Pollock Klinman
Keyword(s):  
Binding Energy ◽  
Amine Oxidase ◽  
Catalytic Efficiency ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase ◽  
Oxidase Reaction

Stereochemistry and kinetic isotope effects in the bovine plasma amine oxidase catalyzed oxidation of dopamine

Biochemistry ◽  
1979 ◽  
Vol 18 (10) ◽  
pp. 1969-1979 ◽  
Author(s):  
Michael C. Summers ◽  
Radmila Markovic ◽  
Judith P. Klinman
Keyword(s):  
Amine Oxidase ◽  
Isotope Effects ◽  
Kinetic Isotope Effects ◽  
Kinetic Isotope ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase ◽  
Catalyzed Oxidation

Mechanism of hydration and isomerisation of 4-ethylidene-2,6-di-tert-butyl-2,5-cyclohexadien-1-one. Kinetics, acid-base catalysis and solvent deuterium isotope effects

1979 ◽  
Vol 44 (1) ◽  
pp. 110-122 ◽  
Author(s):  
Jiří Velek ◽  
Bohumír Koutek ◽  
Milan Souček
Keyword(s):  
Aqueous Medium ◽  
Rate Equation ◽  
Kinetic Data ◽  
Isotope Effects ◽  
Base Catalysis ◽  
Quinone Methide ◽  
Reaction Products ◽  
Acid Base ◽  
Deuterium Isotope Effects ◽  
Hydroxybenzyl Alcohol

Competitive hydration and isomerisation of the quinone methide I at 25 °C in an aqueous medium in the region of pH 2.4-13.0 was studied spectrophotometrically. The only reaction products in the studied range of pH are 4-hydroxybenzyl alcohol (II) and 4-hydroxystyrene (III). The form of the overall rate equation corresponds to a general acid-base catalysis. The mechanism of both reactions for three markedly separated pH regions is discussed on the basis of kinetic data and solvent deuterium effect.

Selective Inhibition of Bovine Plasma Amine Oxidase by Homopropargylamine, a New Inactivator Motif

2004 ◽  
Vol 126 (25) ◽  
pp. 8038-8045 ◽  
Author(s):  
Chunhua Qiao ◽  
Heung-Bae Jeon ◽  
Lawrence M. Sayre
Keyword(s):  
Amine Oxidase ◽  
Selective Inhibition ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase

Copper x-ray absorption spectroscopic studies of the bovine plasma amine oxidase-sulfide complex

1988 ◽  
Vol 27 (21) ◽  
pp. 3859-3861 ◽  
Author(s):  
Robert A. Scott ◽  
Cheryl E. Cote ◽  
David M. Dooley
Keyword(s):  
Amine Oxidase ◽  
Spectroscopic Studies ◽  
X Ray ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase ◽  
X Ray Absorption

scholarly journals Deuterium Isotope Effects on Permeation and Gating of Proton Channels in Rat Alveolar Epithelium

1997 ◽  
Vol 109 (4) ◽  
pp. 415-434 ◽  
Author(s):  
Thomas E. DeCoursey ◽  
Vladimir V. Cherny
Keyword(s):  
Deuterium Oxide ◽  
Isotope Effects ◽  
Ph Dependence ◽  
Channel Gating ◽  
Alveolar Epithelium ◽  
Ionic Species ◽  
Alveolar Epithelial Cells ◽  
Proton Channels ◽  
Deuterium Isotope Effects ◽  
Solvent Isotope

The voltage-activated H+ selective conductance of rat alveolar epithelial cells was studied using whole-cell and excised-patch voltage-clamp techniques. The effects of substituting deuterium oxide, D2O, for water, H2O, on both the conductance and the pH dependence of gating were explored. D+ was able to permeate proton channels, but with a conductance only about 50% that of H+. The conductance in D2O was reduced more than could be accounted for by bulk solvent isotope effects (i.e., the lower mobility of D+ than H+), suggesting that D+ interacts specifically with the channel during permeation. Evidently the H+ or D+ current is not diffusion limited, and the H+ channel does not behave like a water-filled pore. This result indirectly strengthens the hypothesis that H+ (or D+) and not OH− is the ionic species carrying current. The voltage dependence of H+ channel gating characteristically is sensitive to pHo and pHi and was regulated by pDo and pDi in an analogous manner, shifting 40 mV/U change in the pD gradient. The time constant of H+ current activation was about three times slower (τact was larger) in D2O than in H2O. The size of the isotope effect is consistent with deuterium isotope effects for proton abstraction reactions, suggesting that H+ channel activation requires deprotonation of the channel. In contrast, deactivation (τtail) was slowed only by a factor ≤1.5 in D2O. The results are interpreted within the context of a model for the regulation of H+ channel gating by mutually exclusive protonation at internal and external sites (Cherny, V.V., V.S. Markin, and T.E. DeCoursey. 1995. J. Gen. Physiol. 105:861–896). Most of the kinetic effects of D2O can be explained if the pKa of the external regulatory site is ∼0.5 pH U higher in D2O.

The essential histidine residues of bovine plasma amine oxidase

1975 ◽  
Vol 400 (2) ◽  
pp. 451-460 ◽  
Author(s):  
Shigeko Tsurushiin ◽  
Akira Hiramatsu ◽  
Melvin Inamasu ◽  
Kerry T. Yasunobu
Keyword(s):  
Amine Oxidase ◽  
Histidine Residues ◽  
Bovine Plasma ◽  
Plasma Amine Oxidase
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