Ruthenium and iron complexes of dipicolinic acid: Synthesis, solution properties and kinetics of electron transfer reactions with ascorbate ions

1983 ◽  
Vol 36 (12) ◽  
pp. 2377 ◽  
Author(s):  
NH Williams ◽  
JK Yandell
Keyword(s):  
Redox Potential ◽  
Rate Constant ◽  
Dipicolinic Acid ◽  
Acid Synthesis ◽  
Equilibrium Mixture ◽  
A Value ◽  
Inert Electrode ◽  
Ph Range ◽  
Kinetics Of ◽  
Kinetics Of Reduction

Standard potentials of the redox couples [bis(pyridine-2,6-dicarboxylate)MIII]-/2- ([M(dipic)2]-/2-, where M = Fe, Ru, Co) have been determined at 25�C, and ionic strength 0.1M (NaClO4 or KNO3). Kinetics of reduction of the oxidized complexes by ascorbate have also been examined under the same conditions. The [Fe(dipic)2]-/2- potential was found to be 355 � 5 mV. Reduction of [Fe(Fe(dipic)2]- in the pH range 4-6 was shown to occur by reaction with ascorbate monoanion (HA-) with a rate constant of (2.2 � 0.2) × 103 1. mol-1 s-1, and ascorbate dianion(A2-) with a rate constant of (7 � 1) × 108 1. mol-1 s-1. K [Ru(dipic)2] has been synthesized. Spectroscopic and analytical evidence suggest that it is a simple six-coordinate species in the solid and in non-aqueous solvents, but that in water it exists as an equilibrium mixture of at least two species. The redox potential for this mixture was found to be 270 � 10 mV. The major component of this mixture is reduced by A2- with a rate constant of (4.7 � 0.1) × 1081.mol-1 s-1. A value of 747 � 5 mV was measured for the redox potential of the cobalt couple, although equilibration of this system with the inert electrode could be achieved only by using [Fe(bpy)2(CN)2] as a mediator. Kinetics of reduction of [Co(dipic)2]- by ascorbate were complex and not reproducible.

The Kinetics of the Formation of the Primary Lactoperoxidase – Hydrogen Peroxide Compound

1971 ◽  
Vol 49 (10) ◽  
pp. 1165-1171 ◽  
Author(s):  
R. James Maguire ◽  
H. Brian Dunford ◽  
Martin Morrison
Keyword(s):  
Hydrogen Peroxide ◽  
Steady State ◽  
Rate Constant ◽  
Order Rate Constant ◽  
Compound I ◽  
Anomalous Effect ◽  
Peroxide Compound ◽  
A Value ◽  
Ph Range ◽  
Kinetics Of

The kinetics of the formation of the primary lactoperoxidase – hydrogen peroxide compound (compound I) at 25 °C have been studied over the pH range 3.0–10.8 by steady state methods. The second-order rate constant k1 is pH-independent over the pH region investigated, having a value of (9.2 ± 0.9) × 106M−1s−1. An anomalous effect of formate buffer on the kinetics of the formation of compound I is reported.

Oxidation of Nickel(II) and Manganese(II) by Peroxodisulfate in Aqueous Solution in the Presence of Molybdate. Crystal Structure of the (NH4)6[NiMo9O32].6H2O Product

1992 ◽  
Vol 45 (12) ◽  
pp. 1943 ◽  
Author(s):  
SJ Dunne ◽  
RC Burns ◽  
GA Lawrance
Keyword(s):  
Rate Constant ◽  
Linear Dependence ◽  
Ph Dependence ◽  
Order Rate Constant ◽  
X Ray Diffraction ◽  
X Ray ◽  
First Order ◽  
Oxidant Concentration ◽  
Ph Range ◽  
Kinetics Of

Oxidation of Ni2+,aq, by S2O82- to nickel(IV) in the presence of molybdate ion, as in the analogous manganese system, involves the formation of the soluble heteropolymolybdate anion [MMogO32]2- (M = Ni, Mn ). The nickel(IV) product crystallized as (NH4)6 [NiMogO32].6H2O from the reaction mixture in the rhombohedra1 space group R3, a 15.922(1), c 12.406(1) � ; the structure was determined by X-ray diffraction methods, and refined to a residual of 0.025 for 1741 independent 'observed' reflections. The kinetics of the oxidation were examined at 80 C over the pH range 3.0-5.2; a linear dependence on [S2O82-] and a non-linear dependence on l/[H+] were observed. The influence of variation of the Ni/Mo ratio between 1:10 and 1:25 on the observed rate constant was very small at pH 4.5, a result supporting the view that the precursor exists as the known [NiMo6O24H6]4- or a close analogue in solution. The pH dependence of the observed rate constant at a fixed oxidant concentration (0.025 mol dm-3) fits dequately to the expression kobs = kH [H+]/(Ka+[H+]) where kH = 0.0013 dm3 mol-1 s-1 and Ka = 4-0x10-5. The first-order dependence on peroxodisulfate subsequently yields a second-order rate constant of 0.042 dm3 mol-1 s-1. Under analogous conditions, oxidation of manganese(II) occurs eightfold more slowly than oxidation of nickel(II), whereas oxidation of manganese(II) by peroxomonosulfuric acid is 16-fold faster than oxidation by peroxodisulfate under similar conditions.

Open-chain nitrogen compounds. Part XV. A kinetic study of the hydrolysis of 1-aryl-3-aryloxymethyl-3-methyltriazenes and related triazenes

1992 ◽  
Vol 70 (8) ◽  
pp. 2224-2233 ◽  
Author(s):  
Keith Vaughan ◽  
Donald L. Hooper ◽  
Marcus P. Merrin
Keyword(s):  
Rate Constant ◽  
Order Rate Constant ◽  
Buffer System ◽  
Open Chain ◽  
Nucleophilic Displacement ◽  
Ether Oxygen ◽  
Rate Of Hydrolysis ◽  
Electron Withdrawing Group ◽  
Ph Range ◽  
Kinetics Of

The kinetics of hydyrolysis of a series of 1-aryl-3-aryloxymethyl-3-methyltriazenes, Ar-N=N-NMe-CH2OAr′, was studied over the pH range 2–7.5. Reactions were followed by the change in UV absorbance spectra of the triazenes. The aryloxymethyltriazenes decompose more slowly at pH 7.5 than the hydroxymethyltriazenes, Ar-N=NMe-CH2OH; the hydrolysis is favoured by the presence of an electron-withdrawing group in Ar′. A mixed isopropanol/buffer system was developed in order to improve solubility of the aryloxymethyl triazenes. Lowering the pH caused an increase in the rate of hydrolysis and under strongly acidic conditions an electron-withdrawing group in Ar′ actually slows down the reaction. A Hammett plot of the pseudo-first-order rate constant, kobs, is curved, indicating that two or more mechanisms operate simultaneously and that the contribution of each mechanism is substituent-dependent. A plot of kobs vs. [buffer] is linear; the slope of the plot affords the rate constant, kb for the buffer-catalyzed reaction for each substituent. A Hammett plot of kb vs. σ is linear with ρ = +0.55, suggesting that the buffer-catalyzed reaction involves nucleophilic displacement of the phenoxy group by the buffer anion. Further analysis afforded the specific acid-catalyzed rate constants, [Formula: see text], for each substituent; this component of the reaction has a negative ρ, consistent with a mechanism involving protonation at the ether oxygen. The postulation that specific acid catalysis is a component of the reaction mechanism was confirmed by the observation of a solvent deuterium isotope effect, 2.28 > kH/kD > 1.60. Only the p-NO2 and p-CN phenyloxymethyltriazenes showed any spontaneous decomposition.

scholarly journals Kinetics of Reduction of Fe(III) Complexes by Outer Membrane Cytochromes MtrC and OmcA of Shewanella oneidensis MR-1

2008 ◽  
Vol 74 (21) ◽  
pp. 6746-6755 ◽  
Author(s):  
Zheming Wang ◽  
Chongxuan Liu ◽  
Xuelin Wang ◽  
Matthew J. Marshall ◽  
John M. Zachara ◽  
...  
Keyword(s):  
Redox Potential ◽  
Outer Membrane ◽  
Kinetic Data ◽  
Shewanella Oneidensis ◽  
Reorganization Energy ◽  
Second Order ◽  
Metal Species ◽  
Stopped Flow ◽  
Kinetics Of ◽  
Kinetics Of Reduction

ABSTRACT Because of their cell surface locations, the outer membrane c-type cytochromes MtrC and OmcA of Shewanella oneidensis MR-1 have been suggested to be the terminal reductases for a range of redox-reactive metals that form poorly soluble solids or that do not readily cross the outer membrane. In this work, we determined the kinetics of reduction of a series of Fe(III) complexes with citrate, nitrilotriacetic acid (NTA), and EDTA by MtrC and OmcA using a stopped-flow technique in combination with theoretical computation methods. Stopped-flow kinetic data showed that the reaction proceeded in two stages, a fast stage that was completed in less than 1 s, followed by a second, relatively slower stage. For a given complex, electron transfer by MtrC was faster than that by OmcA. For a given cytochrome, the reaction was completed in the order Fe-EDTA > Fe-NTA > Fe-citrate. The kinetic data could be modeled by two parallel second-order bimolecular redox reactions with second-order rate constants ranging from 0.872 μM−1 s−1 for the reaction between MtrC and the Fe-EDTA complex to 0.012 μM−1 s−1 for the reaction between OmcA and Fe-citrate. The biphasic reaction kinetics was attributed to redox potential differences among the heme groups or redox site heterogeneity within the cytochromes. The results of redox potential and reorganization energy calculations showed that the reaction rate was influenced mostly by the relatively large reorganization energy. The results demonstrate that ligand complexation plays an important role in microbial dissimilatory reduction and mineral transformation of iron, as well as other redox-sensitive metal species in nature.

Studies on Horseradish Peroxidase. VII. A Kinetic Study of the Oxidation of Iodide by Horseradish Peroxidase Compound II

1971 ◽  
Vol 49 (18) ◽  
pp. 3059-3063 ◽  
Author(s):  
R. Roman ◽  
H. B. Dunford ◽  
M. Evett
Keyword(s):  
Ionic Strength ◽  
Horseradish Peroxidase ◽  
Kinetic Study ◽  
Rate Constant ◽  
Ph Dependence ◽  
Order Rate Constant ◽  
Acid Dissociation ◽  
Ph Range ◽  
Compound Ii ◽  
Kinetics Of

The kinetics of the oxidation of iodide ion by horseradish peroxidase compound II have been studied as a function of pH at 25° and ionic strength of 0.11. The logarithm of the second-order rate constant decreases linearly from 2.3 × 105 to 0.1 M−1 s−1 with increasing pH over the pH range 2.7 to 9.0. The pH dependence of the reaction is explained in terms of an acid dissociation outside the pH range of the study.

Kinetics of the renneting reaction followed by measurement of turbidity as a function of wavelength

1998 ◽  
Vol 65 (4) ◽  
pp. 545-554 ◽  
Author(s):  
STIG B. LOMHOLT ◽  
PEDER WORNING ◽  
LARS ØGENDAL ◽  
KARSTEN B. QVIST ◽  
DOUGLAS B. HYSLOP ◽  
...  
Keyword(s):  
Rate Constant ◽  
Energy Barrier ◽  
Absolute Temperature ◽  
Degree Of Polymerization ◽  
Average Degree ◽  
Initial Value ◽  
A Value ◽  
Rennet Coagulation ◽  
Smoluchowski’S Equation ◽  
Kinetics Of

In order to describe the kinetics of rennet coagulation, measurements of turbidity as a function of wavelength were used to determine the weight-average degree of polymerization, x¯w, during renneting of milk at three different concentrations of enzyme and three concentrations of casein, including the normal casein concentration of milk. The change of x¯w as a function of time was described using Von Smoluchowski's equation, testing a number of expressions for the aggregation rate constant, kij. The best description was achieved when kij was taken as a function of an energy barrier against aggregation that was diminished by the proteolysis of κ-casein. The initial value of the energy barrier partly depended on the casein concentration, and had a value >25 kBT at normal casein concentration, where kB is Boltzmann's constant and T the absolute temperature. When the proteolysis of κ-casein was complete, the energy barrier was reduced to 11 kBT and was independent of casein concentration.

The Kinetics of the Reaction 2C3H6 → C3H5 + C3H7

1973 ◽  
Vol 51 (17) ◽  
pp. 2934-2939 ◽  
Author(s):  
M. Simon ◽  
M. H. Back
Keyword(s):  
Activation Energy ◽  
Rate Constant ◽  
Radical Scavenger ◽  
A Value ◽  
Kinetics Of

An attempt has been made to measure the rate constant for the bimolecular process[Formula: see text]using acetaldehyde as a radical scavenger. The rate constant obtained may be expressed as follows:[Formula: see text]This activation energy corresponds to a value of 36 kcal/mol for ΔHf(allyl).

scholarly journals The kinetics of oxygen exchange between the sulfite ion and water

1970 ◽  
Vol 48 (13) ◽  
pp. 2035-2041 ◽  
Author(s):  
R. H. Betts ◽  
R. H. Voss
Keyword(s):  
Aqueous Solution ◽  
Ionic Strength ◽  
Rate Constant ◽  
Rate Constants ◽  
Time Rate ◽  
A Value ◽  
First Time ◽  
Kinetics Of ◽  
Sulfite Ion ◽  
Gross Rate

Oxygen of mass 18 was used as a stable tracer to measure the rate of exchange between the sulfite ion and water as a function of pH and total sulfite concentration. A value for the rate constant of hydration of SO2 in aqueous solution was determined. The gross rate constants k1 and k−1 for the overall reaction[Formula: see text]at 24.7 °C and ionic strength = 0.9 were evaluated from exchange results to be [Formula: see text]Also, for the first time, rate constants for the pyrosulfite equilibrium[Formula: see text]Were obtained[Formula: see text]at 24.7 °C and ionic strength = 0.9

The kinetics of the reaction of N,N-dimethyl-2-phenylaziridinium ion with bovine erythrocyte acetylcholinesterase

1970 ◽  
Vol 48 (3) ◽  
pp. 244-250 ◽  
Author(s):  
Jocelyn E. Purdie ◽  
R. M. Heggie
Keyword(s):  
Rate Constant ◽  
Order Rate Constant ◽  
Bovine Erythrocyte ◽  
Acidic Group ◽  
Ph Values ◽  
Order Rate ◽  
Decreasing Ph ◽  
Ph Range ◽  
Kinetics Of ◽  
Hydrolysis Of

The kinetics of the hydrolysis of N,N-dimethyl-2-phenylaziridinium ion (DPA) have been studied over the pH range 5.5–8.0 as have the kinetics of the interaction of DPA with bovine erythrocyte acetyl-cholinesterase. The enzyme is initially inhibited reversibly and subsequently irreversibly towards acetylcholine hydrolysis. The hydrolysis of DPA was found to be pH independent over the range studied while the reversible noncompetitive inhibition increased with increasing pH, the data suggesting the requirement for a basic group on the enzyme with a pKa of about 6.5.Between pH values of 6.0 and 8.0 the kinetics of the irreversible inhibition are consistent with either of two kinetically indistinguishable mechanisms, one involving transformation of the initial reversible complex and the other an independent attack on the uncomplexed enzyme. The first mechanism gives rise to a first-order rate constant which is comparable with that for the hydrolysis of DPA but which increases with decreasing pH; an acidic group on the enzyme with pKa between 6.0 and 7.0 may be involved. The second-order rate constant arising from the second treatment goes through a maximum at pH 7.3. At pH 5.5 the kinetics are not consistent with either mechanism.

The formation and decay of the oxyferrous complex of beef adrenocortical cytochrome P-450scc. Rapid-scan and stopped-flow studies

1987 ◽  
Vol 65 (5) ◽  
pp. 486-492 ◽  
Author(s):  
Mohammed A. Kashem ◽  
H. Brian Dunford
Keyword(s):  
Rate Constant ◽  
Acid Group ◽  
Spontaneous Decay ◽  
Stopped Flow ◽  
Oxygen Binding ◽  
First Order Kinetics ◽  
Rapid Scan ◽  
Ph Range ◽  
Kinetics Of ◽  
Cytochrome P 450

The formation and spontaneous decay of the oxyferrous complex of purified beef adrenocortical cholesterol-bound (high spin) cytochrome P-450scc have been studied by means of rapid-scan spectrometry in the Soret region at 4 °C. The oxyferrous complex, the formation of which occurs within 40 ms with a Soret absorption peak at 422 nm, is unstable and decays spontaneously to the ferric cholesterol-bound cytochrome P-450scc. The rapid-scan spectra for both processes were recorded. Isosbestic points occur at the following wavelengths: between ferrous and oxyferrous complex at 418 nm, between oxyferrous complex and ferric cytochrome P-450scc at 411 nm. The kinetics of oxygen binding and spontaneous decay of the oxyferrous complex have also been studied at 4 °C by means of stopped-flow experiments in the pH range 5.1–8.8. The rate constant for oxygen binding is constant at 5.8 × 105 ± 0.8 × 105 M−1∙s−1 over the pH range of the study. On the other hand, the decay process exhibited pH-dependent monophasic first-order kinetics. The rate constant for the decay appears to be influenced by an acid group with a pKa of 7.1 on the oxyferrous complex of cholesterol-bound cytochrome P-450scc.

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