Electron transfer and autoxidation kinetics of the bis(imidazole)bis(dimethylglyoximato)iron(II) complex

Henrique E. Toma; Antonio Carlos C. Silva

doi:10.1139/v86-212

Electron transfer and autoxidation kinetics of the bis(imidazole)bis(dimethylglyoximato)iron(II) complex

Canadian Journal of Chemistry ◽

10.1139/v86-212 ◽

1986 ◽

Vol 64 (7) ◽

pp. 1230-1235 ◽

Cited By ~ 8

Author(s):

Henrique E. Toma ◽

Antonio Carlos C. Silva

Keyword(s):

Aqueous Solution ◽

Electron Transfer ◽

Cyclic Voltammetry ◽

Stopped Flow ◽

Imidazole Ligand ◽

Autoxidation Reaction ◽

Stopped Flow Kinetics ◽

Kinetics Of

The properties and reactivity of the bis(imidazole)bis-(dimethylglyoximato)iron(II) complex have been studied based on spectroelectrochemistry, cyclic voltammetry, and stopped-flow kinetics in aqueous solution. The autoxidation reaction was found to be inhibited by the imidazole ligand in excess but susceptible to copper(II) catalysis. In this case a mechanism has been proposed, consisting of a rapid electron transfer followed by the reoxidation of the resulting Cu(I) species by O2.

The mechanism of the oxidation of thiocyanate ion by peroxomonosulphate in aqueous solution. II. Kinetics of the reaction

Australian Journal of Chemistry ◽

10.1071/ch9661365 ◽

1966 ◽

Vol 19 (8) ◽

pp. 1365 ◽

Cited By ~ 4

Author(s):

RH Smith ◽

IR Wilson

Keyword(s):

Aqueous Solution ◽

Initial Rate ◽

Stopped Flow ◽

Thiocyanate Ion ◽

First Order ◽

Conductance Method ◽

Rate Of Reaction ◽

Kinetics Of

Initial rates of reaction for the above oxidation have been measured by a stopped-flow conductance method. Between pH 2 and 3.6, the initial rate of reaction, R, is given by the expression R{[HSO5-]+[SCN-]} = {kb+kc[H+]}[HSO5-]0[SCN-]20+ka[H+]-1[HSO5]20[SCN-]0 As pH increases, there is a transition to a pH-independent rate, first order in each thiocyanate and peroxomonosulphate concentrations.

Cation Catalysis of Anion−Anion Electron Transfer in Aqueous Solution: Self-Exchange Reaction Kinetics of Some Hexa- and Octacyanometalate Couples at Variable Pressure

Inorganic Chemistry ◽

10.1021/ic980887o ◽

1999 ◽

Vol 38 (2) ◽

pp. 301-307 ◽

Cited By ~ 36

Author(s):

Peter D. Metelski ◽

Thomas W. Swaddle

Keyword(s):

Aqueous Solution ◽

Electron Transfer ◽

Reaction Kinetics ◽

Exchange Reaction ◽

Variable Pressure ◽

Kinetics Of

Stopped flow kinetics of carbamylcholine binding to membrane bound acetylcholine receptor

Biochemical and Biophysical Research Communications ◽

10.1016/0006-291x(78)91444-4 ◽

1978 ◽

Vol 81 (3) ◽

pp. 955-964 ◽

Cited By ~ 22

Author(s):

U. Quast ◽

M. Schimerlik ◽

M.A. Raftery

Keyword(s):

Acetylcholine Receptor ◽

Stopped Flow ◽

Membrane Bound ◽

Stopped Flow Kinetics ◽

Kinetics Of

ChemInform Abstract: HIGH-PRESSURE STOPPED-FLOW STUDY OF THE KINETICS OF BASE HYDROLYSIS OF THE DICHROMATE ION BY HYDROXIDE ION, AMMONIA, WATER, AND 2,6-LUTIDINE IN AQUEOUS SOLUTION

Chemischer Informationsdienst ◽

10.1002/chin.198410031 ◽

1984 ◽

Vol 15 (10) ◽

Author(s):

P. MOORE ◽

Y. DUCOMMUN ◽

P. J. NICHOLS ◽

A. E. MERBACH

Keyword(s):

Aqueous Solution ◽

High Pressure ◽

Base Hydrolysis ◽

Stopped Flow ◽

Hydroxide Ion ◽

Ammonia Water ◽

Kinetics Of ◽

Hydrolysis Of ◽

Flow Study

Comparative kinetics of carbon dioxide (CO2) absorption into EAE, 1DMA2P and their blends in aqueous solution using the stopped-flow technique

International Journal of Greenhouse Gas Control ◽

10.1016/j.ijggc.2019.102948 ◽

2020 ◽

Vol 94 ◽

pp. 102948 ◽

Cited By ~ 10

Author(s):

Hongxia Gao ◽

Nan Wang ◽

Jigang Du ◽

Xiao Luo ◽

Zhiwu Liang

Keyword(s):

Carbon Dioxide ◽

Aqueous Solution ◽

Stopped Flow ◽

Co2 Absorption ◽

Carbon Dioxide Co2 ◽

Kinetics Of

Stopped-Flow Kinetic Investigations of One-Electron Transfer Reactions of Phenothiazines and Their Radical Cations in Aqueous Solution

Bulletin of the Chemical Society of Japan ◽

10.1246/bcsj.62.3355 ◽

1989 ◽

Vol 62 (10) ◽

pp. 3355-3358

Author(s):

Lakshmanan Venkatasubramanian ◽

Pichai Maruthamuthu

Keyword(s):

Aqueous Solution ◽

Electron Transfer ◽

Radical Cations ◽

Transfer Reactions ◽

Stopped Flow ◽

Electron Transfer Reactions ◽

Kinetic Investigations

High-Pressure Stopped-Flow Study of the Kinetics of Base Hydrolysis of the Dichromate Ion by Hydroxide Ion, Ammonia, Water, and 2,6-Lutidine in Aqueous Solution

Helvetica Chimica Acta ◽

10.1002/hlca.19830660809 ◽

1983 ◽

Vol 66 (8) ◽

pp. 2445-2448 ◽

Cited By ~ 4

Author(s):

Peter Moore ◽

Yves Ducommun ◽

Peter J. Nichols ◽

Andr� E. Merbach

Keyword(s):

Aqueous Solution ◽

High Pressure ◽

Base Hydrolysis ◽

Stopped Flow ◽

Hydroxide Ion ◽

Ammonia Water ◽

Kinetics Of ◽

Hydrolysis Of ◽

Flow Study

ChemInform Abstract: VOLUMES OF ACTIVATION FOR THE ANATION OF PALLADIUM(II) SUBSTITUTED DIENE COMPLEXES BY CHLORIDE ION IN AQUEOUS SOLUTION. A HIGH PRESSURE STOPPED-FLOW INSTRUMENT FOR STUDYING THE KINETICS OF FAST REACTIONS UNDER PRESSURE

Chemischer Informationsdienst ◽

10.1002/chin.198146308 ◽

1981 ◽

Vol 12 (46) ◽

Author(s):

R. VAN ELDIK ◽

D. A. PALMER ◽

R. SCHMIDT ◽

H. KELM

Keyword(s):

Aqueous Solution ◽

High Pressure ◽

Chloride Ion ◽

Stopped Flow ◽

Fast Reactions ◽

Kinetics Of

ChemInform Abstract: LIGHT-INDUCED ELECTRON-TRANSFER REACTIONS. PART 3. KINETICS OF THE OXIDATION REACTION OF OXALATE ION BY PEROXIDISULFATE ION, BEING INDUCED BY IRRADIATION WITH VISIBLE LIGHT OF AN AQUEOUS SOLUTION CONTAINING TRIS(2,2′-BIPYRIDINE)RUTHEN

Chemischer Informationsdienst ◽

10.1002/chin.198523103 ◽

1985 ◽

Vol 16 (23) ◽

Author(s):

M. KIMURA ◽

S. NISHIDA

Keyword(s):

Aqueous Solution ◽

Electron Transfer ◽

Visible Light ◽

Oxidation Reaction ◽

Transfer Reactions ◽

Electron Transfer Reactions ◽

Kinetics Of ◽

Oxalate Ion

Studies on tryptophan residues of Abrus agglutinin. Stopped-flow kinetics of modification and fluorescence-quenching studies

Biochemical Journal ◽

10.1042/bj2430079 ◽

1987 ◽

Vol 243 (1) ◽

pp. 79-86 ◽

Cited By ~ 4

Author(s):

S R Patanjali ◽

M J Swamy ◽

A Surolia

Keyword(s):

Amino Acid ◽

Protein A ◽

Stopped Flow ◽

Amino Acid Residues ◽

Acidic Amino Acid ◽

Native Protein ◽

Tryptophan Residues ◽

Stopped Flow Kinetics ◽

Two Phases ◽

Kinetics Of

The presence of two essential tryptophan residues/molecule was implicated in the binding site of Abrus agglutinin [Patanjali, Swamy, Anantharam, Khan & Surolia (1984) Biochem. J. 217, 773-781]. A detailed study of the stopped-flow kinetics of the oxidation of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues revealed three classes of tryptophan residues in the native protein. A discrete reorganization of tryptophan residues into two phases was observed upon ligand binding. The heterogeneity of tryptophan exposure was substantiated by quenching studies with acrylamide, succinimide and Cs+. Our study revealed the microenvironment of tryptophan residues to be hydrophobic, and also the presence of acidic amino acid residues in the vicinity of surface-localized tryptophan residues.