scholarly journals The kinetics of oxidation of ferroperoxidase by molecular oxygen. A model of a terminal oxidase

1974 ◽  
Vol 141 (1) ◽  
pp. 265-272 ◽  
Author(s):  
Charles F. Phelps ◽  
Eraldo Antonini ◽  
Giorgio Giacometti ◽  
Maurizio Brunori
Keyword(s):  
Computer Simulation ◽  
Rate Constants ◽  
Time Course ◽  
Initial Rate ◽  
Time Range ◽  
Analogue Computer ◽  
Terminal Oxidase ◽  
Kinetics Of Oxidation ◽  
Rate Limiting ◽  
Kinetics Of

1. The decay of oxyferroperoxidase to ferriperoxidase was studied by rapidly mixing solutions of ferroperoxidase with various amounts of oxygen and following the time-course of appearance of oxyferroperoxidase and its subsequent decay to ferriperoxidase by reaction with ferroperoxidase. 2. The scheme can be accommodated by and [Formula: see text] and occurs without detectable intermediates being observed in the millisecond time-range. 3. Analogue-computer simulation of the reaction is in agreement with the initial rate-limiting reaction being an intermolecular, not intramolecular, electron-donating process, and analysis of the data leads to quantitative values for the rate constants of the overall process. 4. The reaction of oxyferroperoxidase with ferroperoxidase is a model of a terminal oxidase, and the results are discussed in terms of the possible importance of this reaction in peroxidase function, and also in the light it throws on autoxidation of haem compounds.

scholarly journals ON THE KINETICS OF POTENTIAL, ELECTROMOTANCE, AND CHEMICAL CHANGE IN THE EXCITABLE SYSTEM OF NERVE

1958 ◽  
Vol 42 (1) ◽  
pp. 193-229 ◽  
Author(s):  
Paul Mueller
Keyword(s):  
Chemical Equilibrium ◽  
Rate Constants ◽  
Time Course ◽  
Chemical Change ◽  
External Source ◽  
Analogue Computer ◽  
Experimental Conditions ◽  
Excitable System ◽  
Total Potential ◽  
Kinetics Of

The kinetics of interaction between potential, chemical equilibrium, and electromotance in the excitable system of nerve are analyzed. The theoretical system has the following properties: It gives rise to two electromotances each of which depends directly on a chemical equilibrium. The equilibria are determined by the potential across the system. After a sudden potential shift the equilibria reach their new value with an exponential time course, the time constant of which is determined by the rate constants of the two reactions. The rate constants are different due to different activation energies. The two electromotances give rise to potentials of opposite sign. The total potential produced by the system is equal to the sum of the two potentials. The two equilibria are thus determined by any externally applied potential as well as by the sum of the internally produced potentials. The dependence of the equilibria on the potential is calculated from first principles. The equations which describe this system are solved by an analogue computer, which gives instantaneous solutions of the total internal potential as a function of time and any voltage applied from an external source. Comparison between recorded and computed action potentials shows excellent agreement under all experimental conditions. The electromotances might originate from a Ca++—Na+—K+ exchange at fixed negative sites in the Schwann cell.

Submerged upflow biotower operation and computer simulation

1994 ◽  
Vol 30 (11) ◽  
pp. 143-146
Author(s):  
Ronald D. Neufeld ◽  
Christopher A. Badali ◽  
Dennis Powers ◽  
Christopher Carson
Keyword(s):  
Computer Simulation ◽  
Benzoic Acid ◽  
Computer Model ◽  
Rate Constants ◽  
Batch Mode ◽  
Operational Conditions ◽  
First Order ◽  
Low Concentrations ◽  
Biological Transformation ◽  
Kinetics Of

A two step operation is proposed for the biodegradation of low concentrations (< 10 mg/L) of BETX substances in an up flow submerged biotower configuration. Step 1 involves growth of a lush biofilm using benzoic acid in a batch mode. Step 2 involves a longer term biological transformation of BETX. Kinetics of biotransformations are modeled using first order assumptions, with rate constants being a function of benzoic acid dosages used in Step 1. A calibrated computer model is developed and presented to predict the degree of transformation and biomass level throughout the tower under a variety of inlet and design operational conditions.

KINETIC STUDIES OF METHYL-BIS-β-CHLOROETHYLAMINE: III. THE KINETICS OF THE DIMERIZATION IN METHANOL

1948 ◽  
Vol 26b (2) ◽  
pp. 175-180 ◽  
Author(s):  
C. A. Winkler ◽  
A. W. Hay ◽  
A. L. Thompson
Keyword(s):  
Rate Constants ◽  
Initial Rate ◽  
Kinetic Studies ◽  
First Order ◽  
Rate Expression ◽  
Principal Reaction ◽  
Kinetics Of ◽  
Rate Controlling Step

The principal reaction of methyl-bis-β-chloroethylamine in methanol is dimerization, which results in one chlorine from each molecule becoming ionic, but this is accompanied by slight alcoholysis. The rate-controlling step is believed to be the first order formation of an ethylenimonium ion which reacts rapidly with one of its kind to form dimer. The rate expression as calculated from initial rate constants is k (initial) = 4.0 × 1013e−19600/RThr.−1.

scholarly journals A study of the oxidation of butan-1-ol and propan-2-ol by nicotinamide-adenine dinucleotide catalysed by yeast alcohol dehydrogenase.

1975 ◽  
Vol 147 (3) ◽  
pp. 541-547 ◽  
Author(s):  
C J Dickenson ◽  
F M Dickinson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Ternary Complexes ◽  
Kinetics Of Oxidation ◽  
Yeast Alcohol Dehydrogenase ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Ph Range ◽  
Rate Limiting ◽  
Kinetics Of ◽  
Flow Experiments

1. The kinetics of oxidation of butan-1-ol and propan-2-ol by NAD+, catalysed by yeast alcohol dehydrogenase, were studied at 25 degrees C from pH 5.5 to 10, and at pH 7.05 from 14 degrees to 44 degrees C, 2. Under all conditions studied the results are consistent with a mechanism whereby some dissociation of coenzyme from the active enzyme-NAD+-alcohol ternary complexes occurs, and the mechanism is therefore not strictly compulsory order. 3. A primary 2H isotopic effect on the maximum rates of oxidation of [1-2H2]butan-1-ol and [2H7]propan-2-ol was found at 25 degrees C over the pH range 5.5-10. Further, in stopped-flow experiments at pH 7.05 and 25 degrees C, there was no transient formation of NADH in the oxidation of butan-1-ol and propan-2-ol. The principal rate-limiting step in the oxidation of dependence on pH of the maximum rates of oxidation of butan-1-ol and propan-2-ol is consisten with the possibility that histidine and cysteine residues may affect or control catalysis.

Oxidation of 1- and 2-acetylnaphthalenes by iodate - a kinetic study

1990 ◽  
Vol 55 (6) ◽  
pp. 1535-1540 ◽  
Author(s):  
Prerepa Manikyamba
Keyword(s):  
Solvent Effect ◽  
Enol Form ◽  
Aqueous Methanol ◽  
Kinetics Of Oxidation ◽  
First Order ◽  
Carbonium Ion ◽  
Rate Limiting Step ◽  
Limiting Step ◽  
Rate Limiting ◽  
Kinetics Of

Kinetics of oxidation of 1- and 2-acetylnaphthalenes by iodate in the presence of sulphuric acid in aqueous methanol has been studied. The reaction is first order with respect to both [iodate] and [acetylnaphthalene]. Solvent effect indicates a cation-dipole type of interaction in the rate limiting step. A mechanism is proposed with a slow attack of IO2+ on enol form of acetylnaphthalene forming an intermediate carbonium ion, which ultimately gives corresponding ω-hydroxyacetylnaphthalene. The higher reactivity of 2-acetyl isomer is attributed to the greater stability of the corresponding carbonium ion than that of 1-acetyl isomer.

KINETICS OF THE OXIDATION OF URANIUM (IV) BY IRON (III) IN AQUEOUS SOLUTIONS OF PERCHLORIC ACID

1955 ◽  
Vol 33 (12) ◽  
pp. 1780-1791 ◽  
Author(s):  
R. H. Betts
Keyword(s):  
Electron Transfer ◽  
Ionic Strength ◽  
Aqueous Solutions ◽  
Perchloric Acid ◽  
Rate Constants ◽  
Kcal Mole ◽  
Kinetics Of Oxidation ◽  
Temperature Coefficients ◽  
Kinetics Of ◽  
Rate Controlling Step

The kinetics of oxidation of uranium (IV) by iron (III) in aqueous solutions of perchloric acid have been investigated at four temperatures between 3.1 °C. and 24.8 °C. The reaction was followed by measurement of the amount of ferrous ion formed. For the conditions (H+) = 0.1–1.0 M, ionic strength = 1.02, (FeIII) = 10−4–10−5 M, and (UIV) = 10−4–10−5 M, the observed rate law is d(Fe2+)/dt = −2d(UIV)/dt[Formula: see text]K1 and K2 are the first hydrolysis constants for Fe3+ and U4+, respectively, and K′ and K″ are pseudo rate constants. At 24.8 °C., K′ = 2.98 sec.−1, and K″ = 10.6 mole liter−1 sec−1. The corresponding temperature coefficients are ΔH′ = 22.5 kcal./mole and ΔH″ = 24.2 kcal./mole. The kinetics of the process are consistent with a mechanism which involves, as a rate-controlling step, electron transfer between hydrolyzed ions.

Kinetics of oxidation of reduced cytochrome c by aquacopper(II) and chlorocopper(II) complexes in the presence of oxygen

1981 ◽  
Vol 34 (1) ◽  
pp. 99 ◽  
Author(s):  
JK Yandell
Keyword(s):  
Reaction Mechanism ◽  
Ionic Strength ◽  
Cytochrome C ◽  
Rate Constants ◽  
Kinetics Of Oxidation ◽  
Ferrocytochrome C ◽  
Kinetics Of

The rate constants for the oxidation of reduced cytochrome c by aquacopper(II) ion, aquachloro- copper(II) ion and aquadichlorocopper(II) were found to be 5.7�0.3 1. mol-1 s-1, 2.3×102 1. mol-1 s-1 and 5.6xl031. mol-1 s-1 respectively at 25�C, ionic strength 0.1 and pH 4.0. At low ratios of aquacopper(II) ion to ferrocytochrome c, when oxygen is required to completely oxidize the cytochrome, the reaction mechanism was found to be complex. No evidence for the involvement of copper bound to the cytochrome was found.

Kinetics and mechanism of oxidation of iodide ion by the molybdenum (VI) – hydrogen peroxide system

1990 ◽  
Vol 68 (9) ◽  
pp. 1499-1503 ◽  
Author(s):  
Conchita Arias ◽  
Fernando Mata ◽  
Joaquin F. Perez-Benito
Keyword(s):  
Hydrogen Peroxide ◽  
Rate Constants ◽  
Reaction Rate ◽  
Sodium Molybdate ◽  
Initial Reaction Rate ◽  
Initial Reaction ◽  
Kinetics Of Oxidation ◽  
Iodide Ion ◽  
Aqueous Perchloric Acid ◽  
Kinetics Of

The kinetics of oxidation of potassium iodide by hydrogen peroxide in aqueous perchloric acid has been studied both in the absence and in the presence of sodium molybdate by means of the initial-rates method. The law found for the total initial reaction rate is[Formula: see text]The activation energies associated with rate constants k1, k2, and k3 are 52 ± 1, 49 ± 1, and 42 ± 3 kJ mol−1, respectively. A mechanism in agreement with the experimental kinetic data is proposed, according to which rate constants k1, k2, and k3 correspond to the oxidations of iodide ion by H2O2, H3O2+ and H2MoO5, respectively. Keywords: catalysis, hydrogen peroxide, iodide ion, kinetics, molybdate ion.

Kinetics of oxidation of cis-bis(ethylenediamine)isothiocyanatonitrocobalt(III) ion with peroxodisulphate

1979 ◽  
Vol 44 (12) ◽  
pp. 3588-3594 ◽  
Author(s):  
Vladislav Holba ◽  
Olga Volárová
Keyword(s):  
Ionic Strength ◽  
Rate Constants ◽  
Oxidation Kinetics ◽  
Reaction Rate ◽  
Salt Effect ◽  
Activation Parameters ◽  
Reaction Products ◽  
Kinetics Of Oxidation ◽  
Thermodynamic Activation Parameters ◽  
Kinetics Of

The oxidation kinetics of cis-bis(ethylenediamine)isothiocyanonitrocobalt(III) ion with peroxodisulphate was investigated in the medium of 0.01 M-HClO4 in dependence on the ionic strength and temperature and the reaction products were identified. Extrapolated values of thermodynamic activation parameters were determined from the temperature dependence of the rate constants extrapolated to zero ionic strength. The distance of the closest approach was estimated for the reacting ions by evaluating the primary salt effect. To elucidate the mechanism, the influence of the cyclic polyether 18-crown-6 on the reaction rate was followed.

Conversion between permeability states of IP3 receptors in cultured smooth muscle cells

1995 ◽  
Vol 269 (3) ◽  
pp. C813-C818 ◽  
Author(s):  
T. Sugiyama ◽  
W. F. Goldman
Keyword(s):  
Rate Constants ◽  
Time Course ◽  
Ip3 Receptors ◽  
A7r5 Cells ◽  
High Conductance State ◽  
Cultured Smooth Muscle Cells ◽  
Induced Changes ◽  
Kinetics Of ◽  
Best Fit ◽  
Conductance State

The kinetics of the effect of inositol 1,4,5-trisphosphate (IP3) on Ca2+ in the sarcoplasmic reticulum (SR) were studied in saponin-permeabilized A7r5 cells. At 0.1 microM, IP3 elicited slow monoexponential declines in SR free Ca2+ concentration ([Ca2+]SR). For IP3 concentration ([IP3]) = 0.2-100 microM, evoked declines in [Ca2+]SR were biphasic and best fit as the sum of two first-order processes with rate constants kfast and kslow. The kfast varied as a function of [IP3] over the range tested, whereas kslow was already maximal when [IP3] = 0.1 microM. To analyze SR Ca2+ release elicited by IP3, the rate constants for IP3-induced changes in the total SR Ca2+ content (kR) were calculated. kR was accurately described only when both [Ca2+]SR and [IP3] were considered together. kR was dependent on IP3 binding to receptors that existed in either of two states, a high-affinity low-conductance state (IP3RH) and a low-affinity high-conductance state (IP3RL). The permeability of IP3RL was 12.28 times larger than that of IP3RH, and the conversion between permeability states as well as changes in both the affinity and cooperativity with which IP3 was bound to IP3RL were mediated by SR Ca2+. This SR Ca(2+)-dependent modulation of the characteristics of IP3 receptors forms the basis for the biphasic time course characteristic of IP3-evoked SR Ca2+ release.

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