Thermodynamics of chelation. II. Iron(II) and zinc(II) complexes of 6-Methylpyridine-2-aldehyde 2'-pyridylhydrazone

1969 ◽  
Vol 22 (11) ◽  
pp. 2333 ◽  
Author(s):  
RW Green ◽  
WG Goodwin
Keyword(s):  
Ionic Strength ◽  
Equilibrium Constants

6-Methylpyridine-2-aldehyde 2?-pyridylhydrazone is a stronger base but weaker ligand than its parent, paphy. Equilibrium constants are reported for seven temperatures from 5� to 60� and over a range of ionic strength. The properties of the ligand are discussed in terms of the derived enthalpies and entropies of reaction.

SOME EQUILIBRIUM CONSTANTS OF TRANSITION METAL HALIDES

1960 ◽  
Vol 38 (10) ◽  
pp. 1827-1836 ◽  
Author(s):  
M. W. Lister ◽  
P. Rosenblum
Keyword(s):  
Ionic Strength ◽  
Transition Metal ◽  
Equilibrium Constant ◽  
Spectrophotometric Method ◽  
Equilibrium Constants ◽  
Cell Voltage ◽  
Metal Halides ◽  
Complex Ions ◽  
Anomalous Variation ◽  
A Cell

Measurements are reported on the formation of complex ions in solutions containing cupric and chloride or bromide ions, and solutions of nickel or cobalt with chloride. In each case the halide was present in very low amount. With copper a spectrophotometric method was used, and a cell voltage method with nickel and cobalt. The ionic strength was kept constant, but the temperature was varied. The data show difficulties of interpretation if it is assumed that only MX+ ions (M is the metal, X is the halogen) are formed, the difficulties arising from the anomalous variation of the equilibrium constant with temperature, and from the general drift of the calculated constants from the e.m.f. measurements. Various explanations are considered and it is shown that postulation of M2X+3 ions is at least a possible explanation.

Honeybee flight muscle phosphoglucose isomerase: matching enzyme capacities to flux requirements at a near-equilibrium reaction

1997 ◽  
Vol 200 (8) ◽  
pp. 1247-1254 ◽  
Author(s):  
J Staples ◽  
R Suarez
Keyword(s):  
Ionic Strength ◽  
Flight Muscle ◽  
Equilibrium Constants ◽  
Muscle Metabolism ◽  
Phosphoglucose Isomerase ◽  
Glycolytic Flux ◽  
Cell Water ◽  
Economical Design ◽  
Equilibrium Reactions ◽  
Low Ionic Strength

In honeybee flight muscle, there are close matches between physiological flux rates and the maximal activities (Vmax; determined using crude homogenates) of key enzymes catalyzing non-equilibrium reactions in carbohydrate oxidation. In contrast, phosphoglucose isomerase (PGI), which catalyzes a reaction believed to be close to equilibrium, occurs at Vmax values greatly in excess of glycolytic flux rates. In this study, we measure the Vmax of flight muscle PGI, the kinetic parameters of the purified enzyme, the apparent equilibrium constants for the reaction and the tissue concentrations of substrate and product. Using the Haldane equation, we estimate that the forward flux capacity (Vf) for PGI required to achieve physiological glycolytic flux rates is between 800 and 1070 units ml-1 cell water, approximately 45­60 % of the empirically measured Vmax of 1770 units ml-1 cell water at optimal pH (8.0) and low ionic strength (no added KCl). When measured at physiological pH (7.0) and ionic strength (120 mmol l-1 KCl) with saturating levels of substrate, PGI activity is 1130 units ml-1 cell water, a value close to the calculated Vf. These results reveal a very close match between predicted and measured PGI flux capacities, and support the concept of an economical design of muscle metabolism in systems working at very high metabolic rates.

THE DISSOCIATION OF α- AND β-LIPOVITELLIN IN AQUEOUS SOLUTION: PART I. EFFECT OF pH, TEMPERATURE, AND OTHER FACTORS

1962 ◽  
Vol 40 (3) ◽  
pp. 363-372 ◽  
Author(s):  
R. W. Burley ◽  
W. H. Cook
Keyword(s):  
Aqueous Solution ◽  
Ionic Strength ◽  
Aqueous Solutions ◽  
Thermodynamic Data ◽  
Equilibrium Constants ◽  
Effect Of Ph ◽  
Reversible Dissociation ◽  
Lipoprotein Concentration ◽  
Irreversible Aggregation ◽  
Increasing Temperature

The effect of pH, temperature, ionic strength, and lipoprotein concentration on the reversible dissociation of α- and β-lipovitellin in aqueous solutions above pH 6 has been examined by ultracentrifugal measurements. Under otherwise similar conditions α- and β-lipovitellin are 50% dissociated at pH 10.5 and 7.8, respectively. Both lipovitellins undergo an irreversible aggregation above about pH 11; β-lipovitellin is sometimes converted to a non-dissociable form upon aging. Dissociation of both lipovitellins decreases with increasing ionic strength and increasing temperature. Although the ultracentrifugal method has limitations, provisional equilibrium constants and thermodynamic data were obtained from it that are comparable with those obtained for certain protein systems.

scholarly journals Fluorimetric studies on the dimerization equilibrium of protoporphyrin IX and its haemato derivative

1983 ◽  
Vol 209 (2) ◽  
pp. 547-552 ◽  
Author(s):  
R Margalit ◽  
N Shaklai ◽  
S Cohen
Keyword(s):  
Ionic Strength ◽  
Fluorescence Quenching ◽  
Fluorescence Intensity ◽  
Salt Concentration ◽  
Equilibrium Constants ◽  
Protoporphyrin Ix ◽  
Constant Ionic Strength ◽  
Aggregation Process ◽  
Buffer Concentration ◽  
Common Anion

The aggregations of protoporphyrin IX and haematoporphyrin IX in aqueous solutions were studied by fluorimetric techniques. Porphyrin concentrations were limited to 0.001-0.1 microM and 0.01-1 microM for protoporphyrin and haematoporphyrin respectively, where dimerization is the dominant aggregation process. The dimerization equilibrium constants (at 25 degrees C, neutral pH, 50 mM-Tris/HCl buffer) were determined to be 3×10(7) M and 4×10(5) M for the proto and the haemato derivatives respectively. The fluorescence intensity of a given protoporphyrin solution (within the range indicated above) was markedly decreased by salts in the system, over the salt concentration range 0.1-7 mM at constant ionic strength, in the sequence CaCl2 greater than MgCl2 greater than KCl greater than NaCl. The direction of this effect, fluorescence quenching, suggests that these salts promote an increase in aggregation. The differences in the magnitudes of the effect, among different salt species sharing a common anion, at constant ionic strength, imply that the effect is cation-specific. In contrast, the fluorescence intensity of a given solution of haematoporphyrin (within the range indicated above) was unaffected by these salts, under similar concentrations, nor was it sensitive to the total buffer concentration, or to the type of buffer in the system.

Ligand scrambling reactions of cyano(thione)gold(I) complexes and determination of their equilibrium constants

2002 ◽  
Vol 80 (10) ◽  
pp. 1279-1284 ◽  
Author(s):  
Saeed Ahmad ◽  
Anvarhusein A Isab ◽  
Herman P Perzanowski
Keyword(s):  
Ionic Strength ◽  
Nmr Spectroscopy ◽  
Key Words ◽  
Equilibrium Constants ◽  
Solvent Polarity ◽  
Approach To Equilibrium ◽  
Initial Concentration ◽  
C Nmr

Ligand scrambling reactions in cyano(thione)gold(I) complexes ([>C=S-Au-CN]) to form [Au(>C=S)2]+ and [Au(CN)2]– species have been investigated for a series of thiones in DMSO using 13C and 15N NMR spectroscopy. Rapid approach to equilibrium occurred and resulted in distinct signals for the [>C=S-Au-CN] and [Au(CN)2]– complexes, both in 13C and 15N NMR. Equilibrium constants (Keq) were determined for scrambling of all the complexes by integrating the CN resonances in the 13C NMR recorded at 298 K. The influence of various factors (initial concentration, ionic strength, temperature, and solvent polarity) on the Keq value was examined for a representative complex (ImtAuCN (Imt = Imidazolidine-2-thione)).Key words: cyanogold(I) complexes, thiones, ligand scrambling, NMR, Keq.

The trans effect in cobalt(III) complexes. Kinetics and mechanism of substitution of cobalt(III) sulphito complexes

1978 ◽  
Vol 31 (3) ◽  
pp. 561 ◽  
Author(s):  
JK Yandell ◽  
LA Tomlins
Keyword(s):  
Ionic Strength ◽  
Water Molecule ◽  
Rate Constants ◽  
Equilibrium Constants ◽  
Ion Concentration ◽  
Nitrite Ion ◽  
Hydrogen Ion Concentration ◽  
Thiocyanate Ion ◽  
Order Rate ◽  
Incoming Ligand

Equilibrium constants K and rate constants kf have been measured, at 25°C and ionic strength of 1.0, for the substitution of the labile water molecule in trans-[aquabis(ethylenediamine)sulphito-cobalt(III)] ion by thiosulphate ion (K = 1.8×102 mol-1 1., kf = 1.27×103 mol-1 1. s-1), thiocyanate ion (2.5×103, 2.75×102), nitrite ion (1.0×103, 2.06×102), azide ion (2.9×102, 2.4×102) ferricyanide ion (-, 1.72×103), hydrogen azide (< 1.2,1.4×10), ammonia (3.0, 6.7) and imidazole (2.6×102, 5.2). ��� The correlation of these rate constants with charge on the incoming ligand, as well as a decrease in the apparent second-order rate constants observed at high concentrations of the anionic ligands, requires a rapid outer-sphere pre-equilibrium step followed by a rate- determining dissociative interchange of the incoming ligand with the bound water molecule. The activation energy of the thiocyanate substitution was found to be 48 kJ mol-1. Aquation of cis- [azidobis(ethylenediamine)-sulphitocobalt(III)] ion, in the range of hydrogen ion concentration between 10-2 and 0.2 M, was found to give the trans-aquasulphito complex with a first-order rate constant consistent with the equation ��������������������������� k = 4.9×10-4[H+]+1.0×10-5 s-1 at 25°C and ionic strength 1.0.

Kinetics and Equilibrium of Binding of Fe3+ by a Fulvic Acid: A Study by Stopped Flow Methods

1975 ◽  
Vol 53 (20) ◽  
pp. 2979-2984 ◽  
Author(s):  
Cooper H. Langford ◽  
Tahir R. Khan
Keyword(s):  
Ionic Strength ◽  
Complex Formation ◽  
Fulvic Acid ◽  
Metal Ion ◽  
Equilibrium Constants ◽  
Acid Dissociation ◽  
Stopped Flow ◽  
Solution Ph ◽  
Sulfosalicylic Acid ◽  
Flow Measurements

The first report of a rate of binding of a metal ion (Fe3+) by a soluble fulvic acid is derived from stopped flow measurements. The rate of complex formation is normal in Wilkins' sense and similar to that for sulfosalicylic acid. Dissociation is slow (t1/2 > 10 s). The binding of Fe3+ by the fulvic acid in acid solution, pH = 1–2.5, was investigated by kinetic analysis in which the reaction of free Fe3+ with sulfosalicylic acid was followed by stopped flow spectrophotometry on a time scale short compared to release of Fe3+ by fulvic acid. Conditional equilibrium constants found were 1.5 ± 0.3 × 104 at pH = 1.5 and 2.5, and 2.8 ± 0.3 × 103 at pH = 1.0 at 25 °C (ionic strength 0.1).

Acid−Base Equilibrium Constants for Glycine in NaClO4, KCl, and KBr at 298 K. Dependence on Ionic Strength

1998 ◽  
Vol 43 (5) ◽  
pp. 876-879 ◽  
Author(s):  
P. Alonso ◽  
J. L. Barriada ◽  
P. Rodríguez ◽  
I. Brandariz ◽  
M. E. Sastre de Vicente
Keyword(s):  
Ionic Strength ◽  
Equilibrium Constants ◽  
Acid Base ◽  
Base Equilibrium ◽  
Acid Base Equilibrium ◽  
Dependence On Ionic Strength

Kinetics and Mechanism of the Reaction of Dichlorotetraaquaruthenium(III) and Thiols

2012 ◽  
Vol 65 (2) ◽  
pp. 113 ◽  
Author(s):  
Suprava Nayak ◽  
Gouri Sankhar Brahma ◽  
K. Venugopal Reddy
Keyword(s):  
Electron Transfer ◽  
Ionic Strength ◽  
Equilibrium Constants ◽  
Activation Parameters ◽  
Kinetics And Mechanism ◽  
Intermediate Complex ◽  
Mechanism Of Formation ◽  
Temperature Range ◽  
Temperature Reduction ◽  
Mechanism Of The Reaction

The formation of an intermediate ruthenium(iii) thiolate complex by the interaction of thiols, RSH (R = glutathione and l-cysteine) and dichlorotetraaquaruthenium(iii), [RuIIICl2(H2O)4]+, is reported in the temperature range 25–40°C. The kinetics and mechanism of formation of the intermediate complex were studied as a function of [RuIIICl2(H2O)4]+, [RSH], pH, ionic strength and temperature. Reduction of the intermediate complex takes place slowly and results in the corresponding disulfides RSSR and [RuIICl2(H2O)4]+. The results are interpreted in terms of a mechanism involving a rate-determining inner-sphere one-electron transfer from RSH to the oxidant used in the present investigation and a comparison of rate and equilibrium constants is presented with activation parameters.

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