Kinetics and Mechanism of Cationic Micelle/Flexible Nanoparticle Catalysis: A Review

2018 ◽  
Vol 43 (1) ◽  
pp. 1-20 ◽  
Author(s):  
Mohammad Niyaz Khan ◽  
Ibrahim Isah Fagge
Keyword(s):  
Rate Increase ◽  
Molecular Level ◽  
Binding Constants ◽  
Exchange Constant ◽  
Interior Region ◽  
Bimolecular Reactions ◽  
Exterior Region ◽  
Different Shapes ◽  
Molecular Origin ◽  
Kinetics Of

The aqueous surfactant (Surf) solution at [Surf] > cmc (critical micelle concentration) contains flexible micelles/nanoparticles. These particles form a pseudophase of different shapes and sizes where the medium polarity decreases as the distance increases from the exterior region of the interface of the Surf/H2O particle towards its furthest interior region. Flexible nanoparticles (FNs) catalyse a variety of chemical and biochemical reactions. FN catalysis involves both positive catalysis ( i.e. rate increase) and negative catalysis ( i.e. rate decrease). This article describes the mechanistic details of these catalyses at the molecular level, which reveals the molecular origin of these catalyses. Effects of inert counterionic salts (MX) on the rates of bimolecular reactions (with one of the reactants as reactive counterion) in the presence of ionic FNs/micelles may result in either positive or negative catalysis. The kinetics of cationic FN (Surf/MX/H2O)-catalysed bimolecular reactions (with nonionic and anionic reactants) provide kinetic parameters which can be used to determine an ion exchange constant or the ratio of the binding constants of counterions.

THE ALTERATION OF INTRACELLULAR ENZYMES: IV. KINETICS OF CATALASE ALTERATION INDUCED BY CHEMICAL AGENTS

1956 ◽  
Vol 34 (1) ◽  
pp. 25-38
Author(s):  
J. Gordin Kaplan ◽  
Woon-Ki Paik
Keyword(s):  
Molecular Level ◽  
Narrow Range ◽  
Intact Cell ◽  
Cellular Level ◽  
Causal Connection ◽  
Rate Limiting Step ◽  
Chemical Agents ◽  
The Difference ◽  
Rate Limiting ◽  
Kinetics Of

The rate with which n-butanol alters the properties of yeast catalase has been studied as a function of temperature and concentration of altering agent. Activation energies for catalase alteration lay within the rather narrow range of 20–23 kcal./mole, thus confirming a prediction made previously on the basis of the difference in energies of activation for heat destruction of altered and unaltered catalases. Alteration by optimal concentration of butanol was a reaction of zero order. Chloroform also altered yeast catalase with an activation energy within this range of μ values. The close agreement in μ values leads us to conclude that the action of these two altering agents, at all concentrations, is characterized by the same rate-limiting step, even though their action differs in other respects. It was concluded that catalase alteration is probably all-or-none on the molecular level, rather than on the cellular level. Alteration was invariably accompanied by a decrease in the size of the treated cells; alteration was sometimes accompanied by changes in the cytochrome spectrum, but there was no causal connection between these two events. These data are consistent with the interfacial hypothesis, which, in its present crude form, pictures alteration as consisting essentially in the desorption of catalase from some intracellular interface at which it is normally bound in the intact cell.

Modeling the Kinetics of Bimolecular Reactions

2006 ◽  
Vol 106 (11) ◽  
pp. 4518-4584 ◽  
Author(s):  
Antonio Fernández-Ramos ◽  
James A. Miller ◽  
Stephen J. Klippenstein ◽  
Donald G. Truhlar
Keyword(s):  
Bimolecular Reactions ◽  
Kinetics Of

Kinetic and spectrophotometric studies of binding of iron(III) by glutathione

1976 ◽  
Vol 54 (20) ◽  
pp. 3192-3199 ◽  
Author(s):  
Tahir R. Khan ◽  
Cooper H. Langford
Keyword(s):  
Complex Formation ◽  
Kinetic Method ◽  
Binding Constants ◽  
Chelating Agent ◽  
Formation Reaction ◽  
Spectrophotometric Data ◽  
Natural Water Chemistry ◽  
Kinetics Of ◽  
Sulfur Containing

In this report, determination of unbound aquo iron species is accomplished by a kinetic method involving reaction with sulfosalicylic acid (SSA) on a time scale which is very short with respect to reaction of SSA with the glutathione complexes of iron. The data are used to calculate conditional binding constants for Fe(III) to glutathione. Binding constants in 0.1 M ionic strength media were obtained between pH 1 and 2.4 by the kinetic method, and near pH = 3 by spectrophotometry and by examination of the ratio of rate of complex formation and dissociation. The conditional binding 'constant' between pH 1 and 3 is represented as pK = −1.96 – 0.50pH. This is consistent with the importance of reactions involving only very limited proton release. Spectrophotometric data show that the —OH group on Fe(OH)2+ is lost on glutathione complexing. Kinetics of the complex formation reaction between aquo iron(III) species and glutathione are slower than rates of reaction of iron(III) with simple ligands.The glutathione system is regarded as a model system important to natural water chemistry because it is a widely distributed biological sulfur-containing chelating agent.

Molecular-Level Kinetic Modeling of Methyl Laurate: The Intrinsic Kinetics of Triglyceride Hydroprocessing

2018 ◽  
Vol 32 (4) ◽  
pp. 5264-5270 ◽  
Author(s):  
Pratyush Agarwal ◽  
Nicholas Evenepoel ◽  
Sulaiman S. Al-Khattaf ◽  
Michael T. Klein
Keyword(s):  
Kinetic Modeling ◽  
Molecular Level ◽  
Methyl Laurate ◽  
Intrinsic Kinetics ◽  
Kinetics Of

scholarly journals Effect of Cationic/Anionic Mixed Micelles on Reaction Kinetics of Alkaline Hydrolysis of Crystal Violet

2019 ◽  
Vol 31 (3) ◽  
pp. 651-655
Author(s):  
Qidist Yilma ◽  
Dunkana Negussa ◽  
Y. Dominic Ravichandran
Keyword(s):  
Crystal Violet ◽  
Alkaline Hydrolysis ◽  
Mixed Micelles ◽  
Sodium Dodecyl ◽  
Binding Constants ◽  
Regression Parameters ◽  
Experimental Values ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Good Agreement

Kinetics of alkaline hydrolysis of crystal violet, a triphenylmethane dye in the micellar environment of cetyltrimethylammonium bromide (CTAB), sodium dodecyl sulfonate (SDS) and binary mixtures of these surfactants was studied. The regression parameters, together with rate constants and binding constants were obtained by analyzing the rate surfactant profiles using cooperativity model. It was observed that the reaction was catalyzed by both surfactants. The catalytic factor increased by 10 times in SDS and 38 times in CTAB indicating that binding of crystal violet to the micellar surface is stronger in pure CTAB than SDS but the strength drastically reduced in the mixtures of the surfactants. Reduction of binding constant became more important as the mole fraction of CTAB was improved in the mixture. The kinetic data were investigated using Piszkiewicz model and Raghavan-Srinivasan model. The data obtained from the models were in good agreement with the experimental values.

Heparin Effects (And Mechanisms) In The α2-Antithrombin Inactivation Of Serine Proteases--Thrombin, Plasmin, And Trypsin

1981 ◽  
Author(s):  
Gerald F Smith ◽  
Jacqueline L Sundboom
Keyword(s):  
Serine Proteases ◽  
Physiological Role ◽  
Binding Constants ◽  
Reaction Rates ◽  
Heparin Therapy ◽  
Common Mechanism ◽  
High Concentration ◽  
Protein Substrates ◽  
Kinetics Of ◽  
Very High

It is important to elucidate the effects of heparin on the α2-antithrombin (ATIII) inactivation of serine proteases in order to understand the pharmacological activity of heparin. We have studied the enzyme kinetics of the ATIII inactivation of these proteases, and the effects of heparin on these interactions, using a common amide peptide substrate and protein substrates. We also studied the interactions of heparin with the three proteases.We conclude that the mechanism of the catalytic effect of heparin (observed at 0. 005 unit/ml) toward the thrombin- ATIII reaction is different from the mechanism whereby heparin (only at very high concentration, e.g., 10 unit/ml) can induce an enhanced rate in the plasmin-ATIII reaction. We conclude that the first mechanism involves a heparinthrombin complex, while the mechanism with plasmin involves a heparin-ATIII complex which forms only at high heparin concentrations. This is consistent with known appropriate binding constants. We found that heparin has no effect on the very rapid inactivation of trypsin by ATIII. We further conclude that there is no common mechanism whereby clinically relevant levels of heparin cause general enhanced ATIII-protease reaction rates.We suggest ATIII depletion during heparin therapy might be avoided by using low heparin levels, which would not allow heparin-ATIII complexes to form, yet which would catalyze the thrombin-ATIII reaction. Our finding that ATIII inactivates trypsin at a rate similar to the heparin-catalyzed thrombin-ATIII reaction suggests a physiological role for ATIII in the control of trypsin-like enzymes.

scholarly journals Surge motion on a floating cylinder in water of finite depth

2003 ◽  
Vol 2003 (57) ◽  
pp. 3643-3656 ◽  
Author(s):  
Dambaru D. Bhatta
Keyword(s):  
Velocity Potential ◽  
Separation Of Variables ◽  
Finite Depth ◽  
Added Mass ◽  
Computational Results ◽  
Complex Matrix ◽  
Interior Region ◽  
Exterior Region ◽  
Damping Coefficients ◽  
Calm Water

We derived added mass and damping coefficients of a vertical floating circular cylinder due to surge motion in calm water of finite depth. This is done by deriving the velocity potential for the cylinder by considering two regions, namely, interior region and exterior region. The velocity potentials for these two regions are obtained by the method of separation of variables. The continuity of the solutions has been maintained at the imaginary interface of these regions by matching the functions and gradients of each solution. The complex matrix equation is numerically solved to determine the unknown coefficients. Some computational results are presented for different depth-to-radius and draft-to-radius ratios.

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