Reactions of halogens with 2,2′-azinobis-(3-ethylbenzothiazole-6-sulphonate): Stopped-flow kinetics of formation of radical cations and dications

1986 ◽  
Vol 97 (2) ◽  
pp. 213-218
Author(s):  
P. Maruthamuthu ◽  
L. Venkatasubramanian ◽  
P. Dharmalingam
Keyword(s):  
Radical Cations ◽  
Stopped Flow ◽  
Kinetics Of Formation ◽  
Stopped Flow Kinetics ◽  
Kinetics Of

Kinetic and Equilibrium Studies of the Reactions of Cyanide Ion with 1,3,5-Trinitrobenzene, 2,4,6-Trinitroanisole, and 2,4,6-Trinitrotoluene in Isopropanol

1974 ◽  
Vol 52 (1) ◽  
pp. 8-17 ◽  
Author(s):  
Leong Huat Gan ◽  
Albert Richard Norris
Keyword(s):  
Standard Enthalpy ◽  
Equilibrium Constants ◽  
Activation Parameters ◽  
Stopped Flow ◽  
Cyanide Ion ◽  
Equilibrium Studies ◽  
Kinetics Of Formation ◽  
Kinetics Of

Equilibrium constants for the formation of 1:1 cyanide ion σ-complexes with 1,3,5-trinitrobenzene, 2,4,6-trinitroanisole, and 2,4,6-trinitrotoluene have been determined spectrophotometrically over a range of temperatures. Standard enthalpy (ΔH0) and entropy (ΔS0) changes associated with each reaction have been evaluated. The kinetics of formation of the σ-complexes have been investigated by means of a stopped-flow technique and the activation parameters characterizing the formation of each complex have been determined. Evidence is presented which indicates the cyanide ion – 2,4,6-trinitroanisole σ-complex formed in isopropanol contains the cyanide ion bonded exclusively at the C-3 position.

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

1987 ◽  
Vol 243 (1) ◽  
pp. 79-86 ◽  
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.

Absorbance and fluorescence stopped-flow kinetics of Rhus laccase and the catalytic reaction sequence

Biochemistry ◽  
1984 ◽  
Vol 23 (9) ◽  
pp. 2049-2056 ◽  
Author(s):  
Finn B. Hansen ◽  
Robert W. Noble ◽  
Murray J. Ettinger
Keyword(s):  
Catalytic Reaction ◽  
Stopped Flow ◽  
Reaction Sequence ◽  
Stopped Flow Kinetics ◽  
Kinetics Of

Stopped-flow kinetics of proton transfer involving cyclopentadiene derivatives

1978 ◽  
Vol 100 (19) ◽  
pp. 6162-6166 ◽  
Author(s):  
Tadashi Okuyama ◽  
Yoshiya Ikenouchi ◽  
Takayuki Fueno
Keyword(s):  
Proton Transfer ◽  
Stopped Flow ◽  
Stopped Flow Kinetics ◽  
Kinetics Of
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