Kinetics of the Initial Steps of Rabbit Psoas Myofibrillar ATPases Studied by Tryptophan and Pyrene Fluorescence Stopped-Flow and Rapid Flow-Quench. Evidence That Cross-Bridge Detachment Is Slower than ATP Binding†

Biochemistry ◽  
2000 ◽  
Vol 39 (25) ◽  
pp. 7508-7520 ◽  
Author(s):  
Robert Stehle ◽  
Corinne Lionne ◽  
Franck Travers ◽  
Tom Barman
Keyword(s):  
Atp Binding ◽  
Stopped Flow ◽  
Rabbit Psoas ◽  
Cross Bridge ◽  
Pyrene Fluorescence ◽  
Rapid Flow ◽  
Kinetics Of

Transient kinetics of ATP hydrolysis by covalently crosslinked actomyosin complex in water and 40% ethylene glycol by the rapid flow quench method

Biochemistry ◽  
1985 ◽  
Vol 24 (14) ◽  
pp. 3814-3820 ◽  
Author(s):  
J. A. Biosca ◽  
F. Travers ◽  
T. E. Barman ◽  
R. Bertrand ◽  
E. Audemard ◽  
...  
Keyword(s):  
Ethylene Glycol ◽  
Atp Hydrolysis ◽  
Transient Kinetics ◽  
Actomyosin Complex ◽  
Rapid Flow ◽  
Kinetics Of ◽  
Quench Method

Stopped-flow and Brownian dynamics studies of electrostatic effects in the kinetics of binding of 7-methyl-GpppG to the protein eIF4E

2000 ◽  
Vol 29 (7) ◽  
pp. 487-498 ◽  
Author(s):  
E. Błachut-Okrasińska ◽  
E. Bojarska ◽  
A. Niedźwiecka ◽  
L. Chlebicka ◽  
E. Darżynkiewicz ◽  
...  
Keyword(s):  
Brownian Dynamics ◽  
Stopped Flow ◽  
Electrostatic Effects ◽  
Kinetics Of

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

1966 ◽  
Vol 19 (8) ◽  
pp. 1365 ◽  
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.

scholarly journals Metal Enolates – Enamines – Enol Ethers: How Do Enolate Equivalents Differ in Nucleophilic Reactivity?

Synthesis ◽  
2019 ◽  
Vol 51 (05) ◽  
pp. 1157-1170 ◽  
Author(s):  
Artem Leonov ◽  
Daria Timofeeva ◽  
Armin Ofial ◽  
Herbert Mayr
Keyword(s):  
Rate Constants ◽  
Correlation Equation ◽  
Stopped Flow ◽  
Quinone Methides ◽  
Enol Ethers ◽  
Reactivity Descriptors ◽  
Silyl Enol Ethers ◽  
Nucleophilic Reactivity ◽  
Kinetics Of ◽  
Least Squares Minimization

The kinetics of the reactions of trimethylsilyl enol ethers and enamines (derived from deoxybenzoin, indane-1-one, and α-tetralone) with reference electrophiles (p-quinone methides, benzhydrylium and indolylbenzylium ions) were measured by conventional and stopped-flow photometry in acetonitrile at 20 °C. The resulting second-order rate constants were subjected to a least-squares minimization based on the correlation equation lg k = s N(N + E) for determining the reactivity descriptors N and s N of the silyl enol ethers and enamines. The relative reactivities of structurally analogous silyl enol ethers, enamines, and enolate anions towards carbon-centered electrophiles are determined as 1, 107, and 1014, respectively. A survey of synthetic applications of enolate ions and their synthetic equivalents shows that their behavior can be properly described by their nucleophilicity parameters, which therefore can be used for designing novel synthetic transformations.

scholarly journals Positive co-operative binding at two weak lysine-binding sites governs the Glu-plasminogen conformational change

1992 ◽  
Vol 285 (2) ◽  
pp. 419-425 ◽  
Author(s):  
U Christensen ◽  
L Mølgaard
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Conformational Change ◽  
Conformational Changes ◽  
Binding Sites ◽  
High Specificity ◽  
Stopped Flow ◽  
Protein Fluorescence ◽  
Lysine Residues ◽  
Kinetics Of

The kinetics of a series of Glu-plasminogen ligand-binding processes were investigated at pH 7.8 and 25 degrees C (in 0.1 M-NaCl). The ligands include compounds analogous to C-terminal lysine residues and to normal lysine residues. Changes of the Glu-plasminogen protein fluorescence were measured in a stopped-flow instrument as a function of time after rapid mixing of Glu-plasminogen and ligand at various concentrations. Large positive fluorescence changes (approximately 10%) accompany the ligand-induced conformational changes of Glu-plasminogen resulting from binding at weak lysine-binding sites. Detailed studies of the concentration-dependencies of the equilibrium signals and the rate constants of the process induced by various ligands showed the conformational change to involve two sites in a concerted positive co-operative process with three steps: (i) binding of a ligand at a very weak lysine-binding site that preferentially, but not exclusively, binds C-terminal-type lysine ligands, (ii) the rate-determining actual-conformational-change step and (iii) binding of one more lysine ligand at a second weak lysine-binding site that then binds the ligand more tightly. Further, totally independent initial small negative fluorescence changes (approximately 2-4%) corresponding to binding at the strong lysine-binding site of kringle 1 [Sottrup-Jensen, Claeys, Zajdel, Petersen & Magnusson (1978) Prog. Chem. Fibrinolysis Thrombolysis 3, 191-209] were observed for the C-terminal-type ligands. The finding that the conformational change in Glu-plasminogen involves two weak lysine-binding sites indicates that the effect cannot be assigned to any single kringle and that the problem of whether kringle 4 or kringle 5 is responsible for the process resolves itself. Probably kringle 4 and 5 are both participating. The involvement of two lysine binding-sites further makes the high specificity of Glu-plasminogen effectors more conceivable.

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