Sequential Domain Unfolding in Phosphoglycerate Kinase: Fluorescence Intensity and Anisotropy Stopped-Flow Kinetics of Several Tryptophan Mutants

Biochemistry ◽  
1995 ◽  
Vol 34 (42) ◽  
pp. 13943-13948 ◽  
Author(s):  
Joseph M. Beechem ◽  
Mark A. Sherman ◽  
Maria T. Mas
Keyword(s):  
Fluorescence Intensity ◽  
Phosphoglycerate Kinase ◽  
Stopped Flow ◽  
Stopped Flow Kinetics ◽  
Kinetics Of

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

Stopped-flow kinetics of the resynthesis of the reactive site peptide bond in kallikrein inhibitor (Kunitz) by β-trypsin

Biochemistry ◽  
1978 ◽  
Vol 17 (9) ◽  
pp. 1675-1682 ◽  
Author(s):  
Ulrich Quast ◽  
Juergen Engel ◽  
Erna Steffen ◽  
Harald Tschesche ◽  
Sigrid Kupfer
Keyword(s):  
Peptide Bond ◽  
Stopped Flow ◽  
Reactive Site ◽  
Kallikrein Inhibitor ◽  
Stopped Flow Kinetics ◽  
Kinetics Of

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

1986 ◽  
Vol 64 (7) ◽  
pp. 1230-1235 ◽  
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.

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