scholarly journals Errors in the evaluation of Arrhenius and van't Hoff plots

1983 ◽  
Vol 209 (1) ◽  
pp. 277-280 ◽  
Author(s):  
T Keleti
Keyword(s):  
Rate Constant ◽  
Arrhenius Plot ◽  
Product Formation ◽  
Hoff Plot

Errors in the numerical values of activation or normal enthalpies, entropies and free enthalpies calculated from Arrhenius or van't Hoff plots, respectively, are due to the neglect of equidimensionality in equations, or to inappropriate approximations. The logarithmization of dimensioned quantities should be avoided, which demands the use of relative concentrations if a change in mole number occurs in the reaction. The application of the Arrhenius plot to enzymic reactions by using Vmax./ET instead of the rate constant of product formation has meaning only if the reaction follows the simplest Michaelis-Menten mechanism; however, the use of the van't Hoff plot using Km is questionable even in the latter case.

Lysine164α of protein farnesyltransferase is important for both CaaX substrate binding and catalysis

2001 ◽  
Vol 360 (3) ◽  
pp. 625-631 ◽  
Author(s):  
Kendra E. HIGHTOWER ◽  
Smita DE ◽  
Carolyn WEINBAUM ◽  
Rebecca A. SPENCE ◽  
Patrick J. CASEY
Keyword(s):  
Rate Constant ◽  
Positive Charge ◽  
Substrate Binding ◽  
Product Formation ◽  
Chemical Mechanism ◽  
Α Subunit ◽  
Protein Farnesyltransferase ◽  
Oncogenic Ras ◽  
Tumour Formation ◽  
Mechanism Of Catalysis

Protein farnesyltransferase (FTase) catalyses the formation of a thioether linkage between proteins containing a C-terminal CaaX motif and a 15-carbon isoprenoid. The involvement of substrates such as oncogenic Ras proteins in tumour formation has led to intense efforts in targeting this enzyme for development of therapeutics. In an ongoing programme to elucidate the mechanism of catalysis by FTase, specific residues of the enzyme identified in structural studies as potentially important in substrate binding and catalysis are being targeted for mutagenesis. In the present study, the role of the positive charge of Lys164 of the α subunit of FTase in substrate binding and catalysis was investigated. Comparison of the wild-type enzyme with enzymes that have either an arginine or alanine residue substituted at this position revealed unexpected roles for this residue in both substrate binding and catalysis. Removal of the positive charge had a significant effect on the association rate constant and the binding affinity of a CaaX peptide substrate, indicating that the positive charge of Lys164α is involved in formation of the enzyme (E)·farnesyl diphosphate (FPP)·peptide ternary complex. Furthermore, mutation of Lys164α resulted in a substantial decrease in the observed rate constant for product formation without alteration of the chemical mechanism. These and additional studies provide compelling evidence that both the charge on Lys164α, as well as the positioning of the charge, are important for overall catalysis by FTase.

Oxidation of nanocrystalline Mo–Si–N and nanolayered Mo–Si–N/SiC coatings

1999 ◽  
Vol 14 (9) ◽  
pp. 3552-3558 ◽  
Author(s):  
P. Torri
Keyword(s):  
Activation Energy ◽  
Water Vapor ◽  
Oxidation Resistance ◽  
Rate Constant ◽  
Arrhenius Plot ◽  
Single Layer ◽  
Water Vapor Atmosphere ◽  
Oxidation Properties ◽  
Sputter Deposited ◽  
Sic Coatings

Oxidation of sputter-deposited nanocrystalline Mo–Si–N (MoSi2.2N2.5) coatings in oxygen–water vapor atmosphere has been studied in the temperature range 400–850 °C. In addition, the oxidation properties of nanolayered Mo–Si–N/SiC coatings at 700 °C were studied and compared to those of single-layer coatings of both components. No pest disintegration was observed in Mo–Si–N up to 200 h of oxidation. A preexponential rate constant of (3.7 ± 0.5) × 109 (1015 atoms/cm2)2/h and activation energy 1.03 ± 0.02 eV were determined from an Arrhenius plot for parabolic oxygen buildup on Mo–Si–N. Up to 20% less oxygen was detected in the oxidized nanolayered coatings compared to either of the components as a single layer, indicating an improvement in oxidation resistance.

The Initial Stages of the Pyrolysis of Dimethyl Ether

1975 ◽  
Vol 53 (18) ◽  
pp. 2742-2747 ◽  
Author(s):  
Philip D. Pacey
Keyword(s):  
Dimethyl Ether ◽  
Rate Constant ◽  
Arrhenius Plot ◽  
Flow System ◽  
Order Rate Constant ◽  
Chain Termination ◽  
Rate Coefficients ◽  
First Order ◽  
Order Rate ◽  
Initiation Reaction

Dimethyl ether was pyrolized in a flow system at 782–936 K and 25–395 Torr with conversions from 0.2–10%. Product analyses were consistent with a simple Rice–Herzfeld mechanism with most chain termination by the recombination of CH3 radicals. The rate coefficients for both the initiation and termination reactions appeared to be slightly pressure dependent. The first-order rate constant for the initiation reaction,[Formula: see text]calculated from the rate of C2H6 formation, was k1 = 1015.0±0.5exp (−318 ± 8 kJ mol−1/RT) s−1, corresponding to ΔHf0(CH3O) = −5 ± 8 kJmol−1. Comparison of CH4 and C2H6 yields enabled calculation of the rate constant for the reaction of CH3 with dimethyl ether. From 373−936 K, the Arrhenius plot for this reaction is a curve.

Presteady-state kinetics of Bacillus 1,3–1,4-β-glucanase: binding and hydrolysis of a 4-methylumbelliferyl trisaccharide substrate

2001 ◽  
Vol 357 (1) ◽  
pp. 195-202
Author(s):  
Mireia ABEL ◽  
Antoni PLANAS ◽  
Ulla CHRISTENSEN
Keyword(s):  
Steady State ◽  
Rate Constant ◽  
Product Formation ◽  
Lag Phase ◽  
Wild Type ◽  
Induced Fit ◽  
Enzyme Substrate ◽  
Kinetics Of ◽  
Hydrolysis Of ◽  
Presteady State Kinetics

In the present study the first stopped-flow experiments performed on Bacillus 1,3–1,4-β-glucanases are reported. The presteady-state kinetics of the binding of 4-methylumbelliferyl 3-O-β-cellobiosyl-β-d-glucoside to the inactive mutant E134A, and the wild-type-catalysed hydrolysis of the same substrate, were studied by measuring changes in the fluorescence of bound substrate or 4-methylumbelliferone produced. The presteady-state traces all showed an initial lag phase followed by a fast monoexponential phase leading to equilibration (for binding to E134A) or to steady state product formation (for the wild-type reaction). The lag phase, with a rate constant of the order of 100s−1, was independent of the substrate concentration; apparently an induced-fit mechanism governs the formation of enzyme–substrate complexes. The concentration dependencies of the observed rate constant of the second presteady-state phase were analysed according to a number of reaction models. For the reaction of the wild-type enzyme, it is shown that the fast product formation observed before steady state is not due to a rate-determining deglycosylation step. A model that can explain the observed results involves, in addition to the induced fit, a conformational change of the productive ES complex into a form that binds a second substrate molecule in a non-productive mode.

The Reaction of Methyl Radicals with Neopentane

1973 ◽  
Vol 51 (15) ◽  
pp. 2415-2422 ◽  
Author(s):  
Philip D. Pacey
Keyword(s):  
Rate Constant ◽  
Flow Reactor ◽  
Arrhenius Plot ◽  
Reactor System ◽  
Methyl Radicals ◽  
Temperature Ranges ◽  
Initiation Reaction ◽  
Good Agreement

Neopentane was pyrolyzed in a flow reactor system at 793–953 K and 20–400 mm Hg. The rate constant for the initiation reaction,[Formula: see text]calculated from the observed C2H6 yield, was 1017.7±0.3 exp (−356 ± 6 kJ mol−1/RT)s−1, in good agreement with earlier determinations in other temperature ranges. The rate constant of the reaction,[Formula: see text]calculated from the observed CH4 and C2H6 yields, was 1010.5 ± 0.1 exp (−67 ± 2 kJ mol−1/RT) 1 mol−1 s−1, four to ten times faster than predicted on the basis of earlier work at 404–608 K. From 404–953 K, the Arrhenius plot for this reaction is strongly curved.

The Reaction of Methyl Radicals with Molecular Hydrogen

1974 ◽  
Vol 52 (21) ◽  
pp. 3665-3670 ◽  
Author(s):  
Peter C. Kobrinsky ◽  
Philip D. Pacey
Keyword(s):  
Rate Constant ◽  
Molecular Hydrogen ◽  
Arrhenius Plot ◽  
Flow System ◽  
Methyl Radicals

Mixtures of neopentane and hydrogen were pyrolyzed in a flow system at 826–968 K and 27–400 mm Hg. Measurements of the yields of CH4 and C2H6 at various conditions enabled calculation of the rate constant for[Formula: see text]at 926 and 829 K. The Arrhenius plot of these and earlier measurements from 372 to 1370 K is a curve, which can be represented by[Formula: see text]

Evidence for reversible intermediate formation in cyclopentenone cycloaddition

1969 ◽  
Vol 47 (4) ◽  
pp. 711-712 ◽  
Author(s):  
P. de Mayo ◽  
A. A. Nicholson ◽  
M. F. Tchir
Keyword(s):  
Rate Constant ◽  
Intermediate Formation ◽  
Product Formation ◽  
A Value

The usual kinetics for product formation lead to variable values of kd, the rate constant for decay of the responsible triplet. On the assumption that at least one intermediate is formed which gives either products, or reverts to starting materials, a value near 108 s−1 is obtained for kd both from cyclopentene and hex-3-ene cycloadditions.

scholarly journals A Two-part Approach to the Determination of Intrinsic Rate Constants of an Alpha-amylase Catalysed Reaction

2020 ◽  
pp. 8-21
Author(s):  
Ikechukwu I. Udema
Keyword(s):  
Rate Constant ◽  
Rate Constants ◽  
Catalytic Efficiency ◽  
Intrinsic Rate ◽  
Product Formation ◽  
Intermolecular Potential ◽  
Diffusion Controlled ◽  
Quantitative Results ◽  
Intrinsic Rate Constant

Background: There is a need for equations with which to calculate the intrinsic rate constants that can further characterise enzyme catalysed reactions despite what seems to be conventional differences in methodology in the literature. Methods: Theoretical, experimental (Bernfeld method), and computational methods. Objectives: 1) To derive an alternative intrinsic rate constant equations consistent with their dimension, 2) derive electrostatic intermolecular potential energy equation, (xe), 3) calculate the intrinsic rate constants for forward (k1) and reverse (k2) reactions, and 4) define the dependence or otherwise of kinetic constants on diffusion and deduce the catalytic efficiency. Results and Discussion: The ultimate quantitative results were ~ 64.69 ±  0.49 exp (+3)/ min (k2) (and kd (s) = ~ 60.66 exp (+3)/ min), ~ 1594.48 ± 11.99 exp (+3) exp (+3) L/mol.min (k1) (and ka (s) = ~1482.47 exp (+3) L/mol.min), ~ 58.00 ± 10.83 exp (+3) /min, the apparent rate constant for reverse reaction (kb), and ~ 75.83 ± 10.83 exp (+3) /min, the rate constant for product formation (k3). The catalytic efficiency was: 3.025 exp (+ 9) L / mol.     Conclusion: The relevant equations were derived. Based on the derived equations the intrinsic rate constants can be calculated. Since k3 is > kb, then k3 is diffusion controlled and it appears that the enzyme has reached kinetic perfection. The evaluation of rate constants either from the perspective of diffusion dependency or independency cannot be valid without Avogadro number.

Kinetics and Mechanism of Growth of β-Solid Solution during Reaction Diffusion in Binary Titanium and Zirconium Alloy Systems

2008 ◽  
Vol 279 ◽  
pp. 117-124 ◽  
Author(s):  
G.P. Tiwari ◽  
Osamu Taguchi ◽  
Yoshiaki Iijima ◽  
G.B. Kale
Keyword(s):  
Solid Solution ◽  
Growth Rate ◽  
Rate Constant ◽  
Growth Kinetics ◽  
Zirconium Alloy ◽  
Arrhenius Plot ◽  
Reaction Diffusion ◽  
Growth Rate Constant ◽  
Satisfactory Description ◽  
Alloy Systems

High temperature beta-phase in titanium and zirconium alloy systems decomposes through an eutectoid reaction into a Ti- and Zr-rich a-solid solution and an intermetallic compound. The present paper reports the layer growth kinetics of the b-solid solution phase in elemental diffusion couples of titanium and zirconium. The growth kinetics obeys a parabolic growth law. However, the temperature dependence of the growth rate constant shows a bimodal behavior. The Arrhenius plot of the growth rate constant, which is linear at the start, becomes curved at lower temperature ranges. The deviation from the Arrhenius plot of the growth rate constant is related to the curvature in the solvus line of the b-solid solution. A theoretical model for the reaction diffusion responsible for the growth of b-solid solution is presented. The growth rate of b-phase is described by the equation 2 2 . . W k D C t b = = b D x , where k is a growth rate constant and Wb is the thickness of the b-phase formed over a period of time t, Db is the interdiffusion coefficient for the b-phase, DC is concentration range of b-phase and x is a parameter which is a function of the miscibility gaps in the phase diagram on the either side of the b-phase. The above equation provides a satisfactory description of the various aspect of the phenomenon of the growth of b-phase in Ti-and Zr-alloy systems.

Kinetics and Mechanistic Study on the Reaction of Iodo(diethylenetriamine) Platinum(II) with L-Cystine

2009 ◽  
Vol 62 (5) ◽  
pp. 493 ◽  
Author(s):  
Trilochan Swain ◽  
Prakash Mohanty
Keyword(s):  
Rate Constant ◽  
Total Concentration ◽  
Formation Rate ◽  
Activation Parameters ◽  
Order Rate Constant ◽  
Product Formation ◽  
Ring Closure ◽  
Mechanistic Study ◽  
Rescue Agent ◽  
Product Formation Rate

Substitution reactions of the complex [Pt(dien)I]+, where dien = diethylenetriamine or 1,5-diamino-3-azapentane, with the sulfur-containing rescue agent l-cystine have been studied in a 1.0 × 10–1 mol dm–3 aqueous perchlorate medium at various temperatures (25–50°C) and pH (2.30–1.00) using a UV-visible spectrophotometer. The products were characterized by their infrared and 1H NMR data at various temperatures. These data indicate that [Pt(dien)I]+ formed a complex with l-cystine through Pt–S bonds at pH 1.00–2.30. This Pt–S bond is observed at 50°C with ring closure of the dien (δ 3.8–3.9, 2H, CH2) and with open-ring dien (δ 3.2, 3.6–3.8 (dien), 2H, CH2). All reactions follow the rate law –d[mixture]/dt = (k1 + k2[Nu])[PtII], where k2 denotes a second-order rate constant and [Nu] is the total concentration of nucleophile. The product formation rate constant and activation parameters Ea, ΔH#, and ΔS# have been determined.

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