Pulse radiolysis of ethanol

1970 ◽  
Vol 48 (11) ◽  
pp. 1645-1650 ◽  
Author(s):  
J. W. Fletcher ◽  
P. J. Richards ◽  
W. A. Seddon
Keyword(s):  
Pulse Radiolysis ◽  
Order Rate Constant ◽  
Radiation Chemistry ◽  
Square Root ◽  
Decay Kinetics ◽  
Solvated Electron ◽  
First Order ◽  
Computer Calculations ◽  
Pseudo First Order ◽  
Positive Ion

The radiation chemistry of ethanol has been investigated by pulse radiolysis with emphasis on the decay kinetics and yield of the solvated electron, e−EtOH, in neutral and alkaline solution. Computer calculations show that the experimental data are most consistent with a yield G(e−EtOH) = 1.7 molecules/100 eV, and a pseudo first-order half life for e−EtOH, [Formula: see text] which corresponds to a second-order rate constant k(e− + EtOH) = 7 × 103 M−1 s−1.Rates of reaction of the electron with acetaldehyde and C6F12 have been determined to be 4.0 ± 0.5 × 109 and 2.5 ± 0.5 × 109 M−1 s−1, respectively.The empirical square root formula for spur scavenging kinetics[Formula: see text]is obeyed for scavenging of the radiation produced positive ion.

Étude par radiolyse pulsée des propriétés spectrales et cinétiques de l'électron solvaté dans l'hexane-1,2,6-triol liquide

1995 ◽  
Vol 73 (1) ◽  
pp. 117-122 ◽  
Author(s):  
J.-P. Jay-Gerin ◽  
J. Chevrel ◽  
C. Ferradini ◽  
E. Ray ◽  
M.H. Klapper ◽  
...  
Keyword(s):  
Absorption Spectrum ◽  
Optical Absorption ◽  
Linear Accelerator ◽  
Pulse Radiolysis ◽  
Order Reaction ◽  
Kinetic Properties ◽  
Solvated Electron ◽  
Solvent Viscosity ◽  
First Order ◽  
Short Times

The optical absorption spectrum of the solvated electron (es−) in liquid hexane-1,2,6-triol has been measured by nanosecond pulse radiolysis at different temperatures (10–40 °C) to investigate the influence of high solvent viscosity values on the spectral and kinetic properties of es−. The wavelength at the absorption maximum, λmax, is equal to 560 nm, and its variation with temperature, if it exists in the considered zone, is less than the experimental error. At 20 °C and 150 ns, the value of the product [Formula: see text] of the yield of es− and the molar extinction coefficient at λmax is 2.55 × 104 molecule/(M cm 100 eV). In the context of this work, we have compared results obtained with both a linear accelerator and a Febetron, a comparison that has allowed us to evaluate the influence of variations of the dose per pulse and to extend measurements to short times. In the case of experiments performed with the linear accelerator, es− is found to decay at all wavelengths by a first-order reaction (or by a pseudo-first-order reaction) with an activation energy of ~45 kJ mol−1. By contrast, kinetic curves obtained with the Febetron seem to show a competition in which a second-order law is followed at short times. The fact that the shape of the spectra seems to vary as a function of the dose per pulse indicates the possible intervention of another species whose formation is favored by the use of high radiation doses. In other respects, the kinetics of electron solvation does not seem to be controlled by the viscosity of the solvent in our experimental conditions. Keywords: liquid hexane-1,2,6-triol, pulse radiolysis, linear accelerator and Febetron, solvated electron, optical absorption spectrum, kinetic properties, solvent viscosity, dose and temperature effects.

Kinetics of reconstitution of apotyrosinase by copper

1990 ◽  
Vol 68 (2) ◽  
pp. 476-479
Author(s):  
Donald C. Wigfield ◽  
Douglas M. Goltz
Keyword(s):  
Rate Constant ◽  
Copper Concentration ◽  
Copper Ions ◽  
Copper Ion ◽  
Order Rate Constant ◽  
First Order ◽  
Order Rate ◽  
Pseudo First Order ◽  
Rate Limiting ◽  
Kinetics Of

The kinetics of the reconstitution reaction of apotyrosinase with copper (II) ions are reported. The reaction is pseudo first order with respect to apoenzyme and the values of these pseudo first order rate constants are reported as a function of copper (II) concentration. Two copper ions bind to apoenzyme, and if the second one is rate limiting, the kinetically relevant copper concentration is the copper originally added minus the amount used in binding the first copper ion to enzyme. This modified copper concentration is linearly related to the magnitude of the pseudo first order rate constant, up to a copper concentration of 1.25 × 10−4 M (10-fold excess), giving a second order rate constant of 7.67 × 102 ± 0.93 × 102 M−1∙s−1.Key words: apotyrosinase, copper, tyrosinase.

scholarly journals Acrolein, an irreversible active-site-directed inhibitor of deoxyribose 5-phosphate aldolase?

1976 ◽  
Vol 153 (2) ◽  
pp. 495-497 ◽  
Author(s):  
D C Wilton
Keyword(s):  
Schiff Base ◽  
Rate Constant ◽  
Active Site ◽  
Order Rate Constant ◽  
Lysine Residue ◽  
Prolonged Incubation ◽  
Enzyme Active Site ◽  
First Order ◽  
Substrate Analogue ◽  
Pseudo First Order

The enzyme deoxyribose 5-phosphate aldolase was irreversibly inactivated by the substrate analogue acrolein with a pseudo-first-order rate constant of 0.324 min-1 and a Ki (apparent) of 2.7 × 10(-4) m. No inactivation was observed after prolonged incubation with the epoxide analogues glycidol phosphate and glycidaldehyde. It is suggested that the acrolein is first activated by forming a Schiff base with the enzyme active-site lysine residue and it is the activated inhibitor that reacts with a suitable-active-site nucleophile.

An automated approach to characterize, in simple kinetic terms, the generation and inactivation of thrombin and the interaction of fibrinogen with thrombin.

1988 ◽  
Vol 34 (10) ◽  
pp. 1971-1975 ◽  
Author(s):  
D R Hoak ◽  
S K Banerjee ◽  
G Kaldor
Keyword(s):  
Prothrombin Time ◽  
Rate Constant ◽  
Thrombin Generation ◽  
Order Rate Constant ◽  
Clinical Use ◽  
First Order ◽  
Pathological Conditions ◽  
Pseudo First Order ◽  
Instantaneous Concentration

Abstract Here, we used a fully automated, computer-directed centrifugal analyzer (which permitted simultaneous turbidimetry and calculation of results) and purified thrombin, fibrinogen, and various inhibitors to study clot formation. The Km and Vm for these reactions were useful in detecting and partly characterizing anticoagulants. We also explored the generation and inactivation of thrombin, using the two-stage prothrombin time and antithrombin activity tests. The amount of thrombin instantaneously generated and inactivated was monitored under artificially created pathological conditions. The pseudo-first-order rate constant for thrombin generation and inactivation and the instantaneous concentration of enzymatically active and inactive thrombin were used in the characterization of these conditions. We believe this approach is suitable for routine clinical use.

Kinetics and mechanisms of oxidations by metal ions. Part IV. Oxidation of phenylphosphinic acid by aquavanadium(V) ions

1985 ◽  
Vol 63 (3) ◽  
pp. 663-666 ◽  
Author(s):  
Raj Narain Mehrotra
Keyword(s):  
Acidic Solution ◽  
Active Form ◽  
Equilibrium Mixture ◽  
Order Rate Constant ◽  
First Order ◽  
Inactive Form ◽  
Pseudo First Order ◽  
Independent Path ◽  
Kinetics Of ◽  
Vanadium Ion

The kinetics of the oxidation of phenylphosphinic acid by quinquevalent vanadium ion have been investigated in aqueous perchlorate media under pseudo-first order conditions (phenylphosphinic acid in excess). The reaction has a first order dependence in [V(V)] and [phenylphosphinic acid] and the observed pseudo-first order rate constant kobs is given by kobs = a + b[H+].The acid-independent path is considered to be due to the reaction between VO2+ (aq.) and C6H5P:(OH)2, the active form of phenylphosphinic acid, while the reaction between V(OH)32+ (aq.) and C6H5P(O)(OH)H, the inactive form of phenylphosphinic acid, is considered to explain the acid-dependent path. Phenylphosphinic acid in aqueous acidic solution is known to exist as an equilibrium mixture of the active and inactive forms. The composite activation and thermodynamic parameters associated with the constants a and b are reported.

scholarly journals Inactivation of the endogenous argininosuccinate lyase activity of duck δ-crystallin by modification of an essential histidine residue with diethyl pyrocarbonate

1993 ◽  
Vol 293 (2) ◽  
pp. 537-544 ◽  
Author(s):  
H J Lee ◽  
S H Chiou ◽  
G G Chang
Keyword(s):  
Enzyme Activity ◽  
Rate Constant ◽  
Order Rate Constant ◽  
Histidine Residue ◽  
Argininosuccinate Lyase ◽  
First Order ◽  
Diethyl Pyrocarbonate ◽  
Order Rate ◽  
Lyase Activity ◽  
Pseudo First Order

The argininosuccinate lyase activity of duck delta-crystallin was inactivated by diethyl pyrocarbonate at 0 degrees C and pH 7.5. The inactivation followed pseudo-first-order kinetics after appropriate correction for the decomposition of the reagent during the modification period. The plot of the observed pseudo-first-order rate constant versus diethyl pyrocarbonate concentration in the range of 0.17-1.7 mM was linear and went through the origin with a second-order rate constant of 1.45 +/- 0.1 M-1.s-1. The double-logarithmic plot was also linear, with slope of 1.13, which suggested a 1:1 stoichiometry for the reaction between diethyl pyrocarbonate and delta-crystallin. L-Arginine, L-norvaline or L-citrulline protected the argininosuccinate lyase activity of delta-crystallin from diethyl pyrocarbonate inactivation. The dissociation constants for the delta-crystallin-L-arginine and delta-crystallin-L-citrulline binary complexes, determined by the protection experiments, were 4.2 +/- 0.2 and 0.12 +/- 0.04 mM respectively. Fumarate alone had no protective effect. However, fumarate plus L-arginine gave synergistic protection with a ligand binding interacting factor of 0.12 +/- 0.02. The double-protection data conformed to a random Uni Bi kinetic mechanism. Fluorescence-quenching studies indicated that the modified delta-crystallin had minimum, if any, conformational changes as compared with the native delta-crystallin. Inactivation of the enzyme activity was accompanied by an increasing absorbance at 240 nm of the protein. The absorption near 280 nm did not change. Treatment of the modified protein with hydroxylamine regenerated the enzyme activity to the original level. These results strongly indicated the modification of an essential histidine residue. Calculation from the 240 nm absorption changes indicated that only one histidine residue per subunit was modified by the reagent. This super-active histidine residue has a pKa value of approximately 6.8 and acts as a general acid-base catalyst in the enzyme reaction mechanism. Our experimental data are compatible with an E1cB mechanism [Raushel (1984) Arch. Biochem. Biophys. 232, 520-525] for the argininosuccinate lyase with the essential histidine residue close to the arginine-binding domain of delta-crystallin. L-Citrulline, after binding to this domain, might form an extra hydrogen bond with the essential histidine residue.

Decolorization of Methyl Orange Simulated Wastewater by Chlorine Dioxide with Ultrasound

2011 ◽  
Vol 255-260 ◽  
pp. 2904-2908
Author(s):  
Li Jie Huang ◽  
Ting Xu ◽  
Shuang Fei Wang
Keyword(s):  
Methyl Orange ◽  
Rate Constant ◽  
Chlorine Dioxide ◽  
Oxidation Process ◽  
Order Rate Constant ◽  
Pseudo First Order Reaction ◽  
First Order ◽  
Effective Technology ◽  
Simulated Wastewater ◽  
Pseudo First Order

Experiments were conducted to investigate the decolorization of methyl orange simulated wastewater in order to assess the effectiveness and feasibility of ultrasound(US) enhanced high-purity chlorine dioxide(ClO2) oxidation process. The results showed that in ClO2/US system the decolorization rate of methyl orange was up to 96%, which was increased by 8% as compared to ClO2treatment alone. The decolorization of methyl orange with/without ultrasonic irradiation follows apparent pseudo-first-order reaction kinetics. The apparent pseudo-first-order rate constant kappwas 0.19min-1in the ClO2/US system, which was a little higher than 0.13min-1of rate constant achieved in ClO2treatment alone. It shows that ClO2/US system can be an effective technology for the decolorization of azo dyes in wastewater.

scholarly journals The reaction of Pseudomonas aeruginosa cytochrome c oxidase with carbon monoxide

1975 ◽  
Vol 151 (1) ◽  
pp. 51-59 ◽  
Author(s):  
S R Parr ◽  
M T Wilson ◽  
C Greenwood
Keyword(s):  
Cytochrome Oxidase ◽  
Flash Photolysis ◽  
Order Rate Constant ◽  
Second Order ◽  
Stopped Flow ◽  
First Order ◽  
Order Rate ◽  
Co Concentration ◽  
Pseudo First Order ◽  
Two Phases

The binding of CO to ascorbate-reduced Pseudomonas cytochrome oxidase was investigated by static-titration, stopped-flow and flash-photolytic techniques. Static-titration data indicated that the binding process was non-stoicheiometric, with a Hill number of 1.44. Stopped-flow kinetics obtained on the binding of CO to reduced Pseudomonas cytochrome oxidase were biphasic in form; the faster rate exhibited a linear dependence on CO concentration with a second-order rate constant of 2 × 10(4) M-1-s-1, whereas the slower reaction rapidly reached a pseudo-first-order rate limit at approx. 1s-1. The relative proportions of the two phases observed in stopped-flow experiments also showed a dependency on CO concentration, the slower phase increasing as the CO concentration decreased. The kinetics of CO recombination after flash-photolytic dissociation of the reduced Pseudomonas cytochrome oxidase-CO complex were also biphasic in character, both phases showing a linear pseudo-first-order rate dependence on CO concentration. The second-order rate constants were determined as 3.6 × 10(4)M-1-s-1 and 1.6 × 10(4)M-1-s-1 respectively. Again the relative proportions of the two phases varied with CO concentration, the slower phase predominating at low CO concentrations. CO dissociation from the enzyme-CO complex measured in the presence of O2 and NO indicated the presence of two rates, of the order of 0.03s-1 and 0.15s-1. When sodium dithionite was used as a reducing agent for the Pseudomonas cytochrome oxidase, the CO-combination kinetics observed by both stopped flow and flash photolysis were extremely complex and not able to be simply analysed.

scholarly journals Mechanism-based inactivation of gastric peroxidase by mercaptomethylimidazole

1993 ◽  
Vol 296 (1) ◽  
pp. 79-84 ◽  
Author(s):  
U Bandyopadhyay ◽  
D K Bhattacharyya ◽  
R K Banerjee
Keyword(s):  
Ph Dependence ◽  
Order Rate Constant ◽  
Order Kinetic ◽  
First Order ◽  
First Order Kinetics ◽  
Mechanism Of Inhibition ◽  
Catalytically Active ◽  
Pseudo First Order ◽  
Inactivation Process ◽  
Gastric Peroxidase

The mechanism of inhibition of gastric peroxidase (GPO) activity by mercaptomethylimidazole (MMI), an inducer of gastric acid secretion, has been investigated. Incubation of purified GPO with MMI in the presence of H2O2 results in irreversible inactivation of the enzyme. No significant inactivation occurs in the absence of H2O2 or MMI, suggesting the involvement of peroxidase-catalysed oxidized MMI (MMIOX.) in the inactivation process. The inactivation follows pseudo-first-order kinetics consistent with a mechanism-based (suicide) mode. The pseudo-first-order kinetic constants at pH 8 are ki = 111 microM, k(inact.) = 0.55 min-1 and t1/2 = 1.25 min, and the second-order rate constant is 0.53 x 10(4) M-1 x min-1. Propylthiouracil also inactivates GPO activity in the same manner but its efficiency (k(inact./ki = 0.46 mM-1 x min-1) is about 10 times lower than that of MMI (k(inact./ki = 5 mM-1 x min-1). The rate of inactivation with MMI shows pH-dependence with an inflection point at 7.3, indicating the involvement in the inactivation process of an ionizable group on the enzyme with a pKa of 7.3. The enzyme is remarkably protected against inactivation by micromolar concentrations of electron donors such as iodide and bromide but not by chloride. Although GPO oxidizes MMI slowly, iodide stimulates it through enzymic generation of I+ which is reduced back to I- by MMI. Although MMIOX. is formed at a much higher rate in the presence of I-, a constant concentration of I- maintained via the reduction of I+ by MMI, protects the active site of the enzyme against inactivation. We suggest that MMI inactivates catalytically active GPO by acting as a suicidal substrate.

Kinetic Study on the Esterification of Hexanoic Acid with N,N-Dialkylamino Alcohols: Evidence for an Activation by Hydrogen Bonding

2006 ◽  
Vol 61 (5) ◽  
pp. 583-588 ◽  
Author(s):  
Stefan Breitenlechner ◽  
Thorsten Bach
Keyword(s):  
Hydrogen Bonding ◽  
Rate Increase ◽  
Order Rate Constant ◽  
Hexanoic Acid ◽  
Hydroxyl Groups ◽  
First Order ◽  
Moderate Rate ◽  
Pseudo First Order ◽  
Related Compounds ◽  
Membered Transition State

The pseudo-first order rate constant for the esterification of hexanoic acid (1) and five different N,N-dialkylamino alcohols (2) was determined in comparison to 1-hexanol (k = 0.67 · 10−5 s−1). The values range from 0.60 · 10−5 s−1 to 9.3 · 10−5 s−1. The data suggest a differing reactivity for structurally related compounds, which is directly correlated to the ability of the corresponding amino alcohol to activate the carboxylic acid by hydrogen bonding. A seven-membered transition state C≠ is postulated for reactions of 2-amino alcohols. The fastest reaction was observed for trans-2-(N,N-dimethylamino) cyclohexanol (2e), in which the amino and the hydroxyl groups are in an almost perfect synperiplanar 1,2-position. Attempts to further enhance the rate of the esterification by the addition of potential catalysts failed. Only Cu(OTf)2 (2.5 mol-%) allowed for a moderate rate increase from 7.5 · 10−5 s−1 (uncatalyzed) to 14.8 · 10−5 s−1 (catalyzed) in the esterification of hexanoic acid (1) with 2-(N,N-dimethylamino)ethanol (2a).

Sign in / Sign up

Export Citation Format

Share Document