scholarly journals Metal Ions and Hydrogen Peroxide. XXV

1972 ◽  
Vol 27 (2) ◽  
pp. 95-100 ◽  
Author(s):  
Peter Waldmeier ◽  
Bernhard Prijs ◽  
Helmut Sigel
Keyword(s):  
Hydrogen Peroxide ◽  
Ionic Strength ◽  
Metal Ions ◽  
Experimental Evidence ◽  
Initial Rate ◽  
Reaction Order ◽  
Ph Dependence ◽  
Initial Concentration ◽  
Ph Dependent ◽  
Ph Range

The decomposition of H2O2, catalyzed by the Co2® complex of 4,4′,4″,4″′-tetrasulfophthalocyanine (CoIIPTS), was investigated in the pH range 3.8 through 10 by measuring the initial rate, v0=d(O2)/dt, of the increasing formation of O2 (25°; I=0.1). In this pH range v0 is proportional to the initial concentration of H2O2 (determined at pH 5.0 and 9.2). Due to the dimerization (log KD=5.47 ±0.09 at natural ionic strength and about 7.63 ±0.16 in 0.1 M NaClO4; 25°) and polymerization of CoIIPTS the catalyst and its reaction order are difficult to establish: Based on the experimental evidence it is suggested that v0 is proportional to the concentration of monomer CoIIPTS. Additionally, there is evidence that the experimentally determined v0 contains the contributions of a pH-independent and a pH-dependent reaction course. These results are analog to those obtained earlier with FeIIIPTS as catalyst. A mechanism for the catalyzed disproportionation of H2O2 by CoIIPTS is proposed. The catalase-like activity of CoIIIPTS (OH) is smaller than that of CoIIPTS and the pH-dependence is different.

scholarly journals Local pH-dependent conformational changes leading to proteolytic susceptibility of cystatin C

1994 ◽  
Vol 302 (2) ◽  
pp. 411-416 ◽  
Author(s):  
P J Berti ◽  
A C Storer
Keyword(s):  
Ionic Strength ◽  
Conformational Change ◽  
Cystatin C ◽  
Conformational Changes ◽  
Ph Dependence ◽  
Significant Proportion ◽  
Cysteine Protease Inhibitor ◽  
Ionic Strength Dependence ◽  
Ph Dependent ◽  
Ph Range

Cystatin C, a cysteine protease inhibitor, was subject to hydrolysis at two sites when complexed with papain and in the presence of excess papain. A pH-dependent cleavage at His-86 increases Asp-87 was observed, as well as a pH-independent one at Gly-4 increases Lys-5. His-86 increases Asp-87 hydrolysis increased with decreasing pH and was characterized kinetically. It could be described by a single ionization with pKa = 3.4 +/- 0.2 and (kcat./Km)max. = 1.4 (+/- 0.4) x 10(4) M-1.s-1 at I = 0.3 M. C.d. spectroscopy, also at I = 0.3 M, demonstrated a conformational change with pKa = 3.2 +/- 0.2, indicating that the pH-dependence of hydrolysis was due to a conformational change in cystatin C. At I = 0.15 M, the pKa of the conformational change observed by c.d. shifted to 4.1 +/- 0.1. This indicates that at physiological ionic strength of 0.15 M, a significant proportion of cystatin C complexed with protease would be in a proteolytically labile conformation over the pH range 4.5 to 5, which is encountered in lysosomes. This may constitute a mechanism for clearing inappropriately localized cystatins. A pH-dependent conformational variability in this region of the inhibitor could explain the differences in the X-ray crystallographic and n.m.r. structures of the homologous chicken cystatin. The ionic-strength dependence of ionization indicates a hydrophobic stabilization of the ionizable group. The lack of pH-dependence of hydrolysis at Gly-4 increases Lys-5, with kcat./Km = 220 +/- 41 M-1.s-1 in the pH range 3.89 to 7.96 was unexpected in light of the normal, bell-shaped pH-dependence of papain-catalysed hydrolyses. This may reflect a different rate-limiting step of cystatin C hydrolysis.

Why is the hydrolytic activity of acetylcholinesterase pH dependent? Kinetic study of acetylcholine and acetylthiocholine hydrolysis catalyzed by acetylcholinesterase from electric eel

2018 ◽  
Vol 73 (9-10) ◽  
pp. 345-351 ◽  
Author(s):  
Alena Komersová ◽  
Markéta Kovářová ◽  
Karel Komers ◽  
Václav Lochař ◽  
Alexander Čegan
Keyword(s):  
Catalytic Activity ◽  
Ionic Strength ◽  
Ph Value ◽  
Hydrolytic Activity ◽  
Initial Substrate ◽  
Electric Eel ◽  
Value Range ◽  
Ph Dependent ◽  
Ph Range ◽  
Initial Substrate Concentration

AbstractThe dependence of the activity of acetylcholinesterase from electric eel at a pH value range of 4.8–9.8 (phosphate buffer), regarding acetylcholine and acetylthiocholine hydrolysis, was determined at 25 °C, ionic strength of 0.11 M, and initial substrate concentration of 4 mM. At a pH range of 4.8–9.8, the dependencesA(pH) form a sigmoid increasing curve with the maximum catalytic activity at a pH range 8–9.5. For acetylcholine hydrolysis, the kinetic reason for such an increase inAconsists mainly of an increase in the rate constantk2(Michaelis-Menten) model with increasing pH of the reaction mixture. For acetylthiocholine hydrolysis, the kinetic explication of the determined dependenceA(pH) is more complicated.

Some Physicochemical Peculiarities of Poplar Plastocyanins a and b

2009 ◽  
Vol 64 (5-6) ◽  
pp. 399-404 ◽  
Author(s):  
Petya K. Christova ◽  
Anthony A. Donchev ◽  
Alexandra C. Shosheva ◽  
Vladimir I. Getov ◽  
Mitko I. Dimitrov
Keyword(s):  
Plant Species ◽  
Ph Dependence ◽  
Equilibrium Constants ◽  
The Other ◽  
Redox Potentials ◽  
Extinction Coefficients ◽  
Structural Differences ◽  
Ph Dependent ◽  
Ph Range ◽  
Reduced Forms

The redox potentials of poplar plastocyanins a and b (PCa, PCb) were determined by spectro photometric titrations of their reduced forms with [Fe(CN)6]3-. It was found that the two isoforms have the following millimolar extinction coefficients ε597, equilibrium constants Keq of one-electron exchange with [Fe(CN)6]4-/[Fe(CN)6]3-, and standard electron potentials E0′: PCa: ε597 = (4.72 ± 0.08) mM-1 cm-1, Keq = 0.133 ± 0.009, E0′ = (354 ± 11) mV; PCb: ε597 = (5.23 ± 0.16) mM-1 cm-1, Keq = 0.175 ± 0.010, E0′ = (363 ± 12) mV. The pH dependence of the redox potential of PCb was studied too. It was found, that the value of E0′ for PCb is constant in the pH range 6.5 - 9.5, but decreases in the range 4.8 - 6.5. On the whole, the dependence resembles that of PC from some well-known plant species, including poplar PCa. The changes of E0′ in the pH-dependent region for poplar PCb, however, are smaller and are 13 mV per pH unit, whereas in the other well-known plant species the changes are about 50 - 60 mV per pH unit. It has been assumed that the weaker pH dependence of E0′ of PCb accounts for some structural differences between PCa and PCb

Vulcanization of Elastomers. 26. Vulcanization of Natural and Synthetic Rubbers by Sulfur in the Presence of Organic Bases

1960 ◽  
Vol 33 (3) ◽  
pp. 834-845
Author(s):  
Walter Scheele ◽  
Wolfgang Redetzky
Keyword(s):  
Initial Rate ◽  
Reaction Order ◽  
Research Work ◽  
Intermediate Compound ◽  
Sulfur Concentration ◽  
Kcal Mole ◽  
Initial Concentration ◽  
Organic Bases ◽  
Single Power ◽  
Theory And Experiment

Abstract In connection with earlier research work, we have carefully studied the decrease of sulfur during the vulcanization of Perbunan N 2818 in the presence of DPG, at various temperatures and with varied molar concentrations of sulfur and accelerator. We found : 1. The sulfur concentration decreases at all temperatures according to a time law of order 0.8. An activation energy of about 28 kcal/mole is derived from the temperature dependence of the rate constant. 2. The reaction order is independent of the initial concentration of reactants. 3. A discrepancy is found in the order of the reaction with respect to time and with respect to concentration, and it is clearly shown that the dependence of the initial rate on the initial concentration can not be expressed by a single power law. 4. The attempt is made to explain the discrepancy by postulating catalysis by an intermediate compound. The consequences from this consideration are compared with the experimental results, and, on the whole, agreement is found between theory and experiment.

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.

Humate Complexation of Neptunium(V) and its Modeling

1994 ◽  
Vol 353 ◽  
Author(s):  
Hirotake Moriyama ◽  
Yasuhiro Nakata ◽  
Kunio Higashi
Keyword(s):  
Functional Groups ◽  
Ph Dependence ◽  
Complexation Constants ◽  
Complexation Constant ◽  
Ph Dependent ◽  
Ph Range

AbstractThe complexation behavior of Np(V) with humate was investigated by spectrophotometry in the pH range from 5.7 to 10 in 0.01–0.5M NaClO4. The absorption peaks of NpO2+ and Np(V) humate were observed at 979.6nm and 989.9nm, respectively, and the apparent complexation constant of the Np(V) humate was found to be pH-dependent. A two-site complexation model was applied to the interpretation of the observed pH-dependence by considering the participation of the two functional groups of carboxylate and phenolate. The dissociation and complexation constants of both functional groups were determined.

An Infrared Spectroscopic Study of the Hydrogen-Deuterium Exchange of Bovine Submaxillary Mucin

1969 ◽  
Vol 23 (3) ◽  
pp. 245-248 ◽  
Author(s):  
Frank S. Parked ◽  
Martin H. Stryker
Keyword(s):  
Ph Dependence ◽  
Spectroscopic Method ◽  
Deuterium Exchange ◽  
Infrared Spectroscopic Study ◽  
Hydrogen Deuterium Exchange ◽  
Infrared Spectroscopic ◽  
Hydrogen Deuterium ◽  
Bovine Submaxillary Mucin ◽  
Ph Dependent ◽  
Ph Range

An infrared spectroscopic method was used to study the hydrogen-deuterium exchange of a glycoprotein, bovine submaxillary mucin (BSM), dissolved in D2O. The pH-dependence of the rate and extent of the H—D exchange of BSM was determined. The rate constant of the exchange decreased as pH increased from 3.7 to 5.3 and remained constant at a minimum value, (0.82 ± 0.09) X 10−2 min−1, from pH 5.3 to 7.2. The extent of the exchange decreased with increasing pH in the pH range 3.7 to 5.3 and levelled off from pH 5.3 to 7.2. It is suggested that these results are due to a pH-dependent conformational change.

Kinetic study of the reaction between cystine and sulfide in alkaline solutions

1987 ◽  
Vol 65 (4) ◽  
pp. 770-774 ◽  
Author(s):  
David K. Liu ◽  
S. G. Chang
Keyword(s):  
Hydrogen Sulfide ◽  
Amino Acid ◽  
Ionic Strength ◽  
Rate Constants ◽  
Amino Acid Analysis ◽  
Ph Dependence ◽  
Alkaline Solutions ◽  
Visible Spectroscopy ◽  
Uv Visible ◽  
Ph Dependent

The reaction between cystine (CySSCy) and hydrogen sulfide ion (HS−) in alkaline solutions has been studied by amino acid analysis and uv–visible spectroscopy. The reaction occurs in two reversible steps to form cysteine (CySH), S-thiocysteine (CySS−), and disulfide (S22−), as represented by the reactions [Formula: see text] and [Formula: see text]. The equilibrium and rate constants were pH dependent due to the presence of various charge types of reactants and products. The rate constants at 25 °C, pH 10.0, and μ = 0.17 M were determined to be: k1 = 3.7 ± 0.4 M−1 min−1, k−1 = 5.5 ± 0.6 M−1 min−1, k2 = 6.1 ± 0.5 M−1 min−1, and k−2 = 122 ± 20 M−1 min−1. When the rate constant k1 is expressed as k1 = A exp (−Ea/RT), values of A = (4.7 ± 0.3) × 1011 M−1 min−1 and Ea = 15.8 ± 0.9 kcal mol−1 were obtained. The ionic strength and pH dependence of k1 were also studied.

scholarly journals pH dependent octanol–water partitioning coefficients of microcystin congeners

2018 ◽  
Vol 16 (3) ◽  
pp. 340-345 ◽  
Author(s):  
James McCord ◽  
Johnsie R. Lang ◽  
Donna Hill ◽  
Mark Strynar ◽  
Neil Chernoff
Keyword(s):  
Algal Blooms ◽  
Environmental Fate ◽  
Ph Dependence ◽  
Significant Heterogeneity ◽  
Algal Toxins ◽  
Amino Acid Region ◽  
Log Kow ◽  
Partitioning Coefficients ◽  
Ph Dependent ◽  
Ph Range

Abstract Hazardous algal blooms can generate toxic compounds with significant health impacts for exposed communities. The ubiquitous class of algal toxins known as microcystins exhibits significant heterogeneity in its peptide structure, which has been minimally studied, given the significant impact this has on hydrophobicity, acid/base character and related environmental fate and health effects. Octanol–water partition coefficients for the microcystin congeners MCLR, MCRR, MCLY, MCLF, and MCLA were calculated over an environmentally and physiologically relevant pH range. Microcystin-LR log(Kow) partition coefficient values were found to be consistent with previously established literature values, 1.67 to −1.41 between pH 1 and 8. Microcystin RR was found to be pH insensitive with a log(Kow) of −0.7. The remaining congeners exhibit similar pH dependence as MCLR, with systematic increases in hydrophobicity driven by the introduction of more hydrophobic residues to their variable amino acid region. The variation in pH dependent hydrophobicity suggests increased propensity for bioaccumulation and alternate environmental fates for differing microcystin forms, requiring further investigation.

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