Kinetic studies on the complex formation of iron(III) with 4-isopropyltropolone by a high-pressure stopped-flow technique. Mechanistic difference between the hexaaquairon(III) ion and the pentaaquamonohydroxoiron(III) ion in their complexation

1983 ◽  
Vol 22 (2) ◽  
pp. 194-198 ◽  
Author(s):  
Koji Ishihara ◽  
Shigenobu Funahashi ◽  
Motoharu Tanaka
Keyword(s):  
High Pressure ◽  
Complex Formation ◽  
Kinetic Studies ◽  
Stopped Flow

scholarly journals KINETIC STUDY ON ANIONIC σ-COMPLEX FORMATION BETWEEN 2,4,6-TRINITROANISOLE AND METHOXIDE ION BY HIGH PRESSURE STOPPED-FLOW METHOD

1979 ◽  
Vol 8 (6) ◽  
pp. 671-674 ◽  
Author(s):  
Noboru Takisawa ◽  
Muneo Sasaki ◽  
Fujitsugu Amita ◽  
Jiro Osugi
Keyword(s):  
High Pressure ◽  
Complex Formation ◽  
Kinetic Study ◽  
Stopped Flow ◽  
Flow Method ◽  
Methoxide Ion

High-pressure stopped-flow study of complex formation on nickel(II) ion in dimethylformamide. Possible existence of a 5-coordinate intermediate

1984 ◽  
Vol 23 (25) ◽  
pp. 4341-4345 ◽  
Author(s):  
Peter J. Nichols ◽  
Yolande Fresard ◽  
Yves Ducommun ◽  
Andre E. Merbach
Keyword(s):  
High Pressure ◽  
Complex Formation ◽  
Stopped Flow ◽  
Flow Study

Kinetic Studies on the ES-complex Formation of p-Hydroxybenzoate Hydroxylase Using the Stopped-flow Method

1970 ◽  
Vol 67 (5) ◽  
pp. 749-752 ◽  
Author(s):  
NAOKI HIGASHI ◽  
HIROHUMI SHOUN ◽  
KEITARO HIROMI ◽  
KEIJI YANO ◽  
KEI ARIMA
Keyword(s):  
Complex Formation ◽  
Kinetic Studies ◽  
Stopped Flow ◽  
Flow Method ◽  
Hydroxybenzoate Hydroxylase

High-Pressure Stopped-Flow Spectrometer for Kinetic Studies of Fast Reactions by Absorbance and Fluorescence Detection

1996 ◽  
Vol 68 (17) ◽  
pp. 3045-3049 ◽  
Author(s):  
Pascal Bugnon ◽  
Gábor Laurenczy ◽  
Yves Ducommun ◽  
Pierre-Yves Sauvageat ◽  
André E. Merbach ◽  
...  
Keyword(s):  
High Pressure ◽  
Fluorescence Detection ◽  
Kinetic Studies ◽  
Stopped Flow ◽  
Fast Reactions

scholarly journals Kinetic Studies on the Enzyme-substrate Complex Formation of p-Hydroxybenzoate Hydroxylase by the Stopped-flow Method

1972 ◽  
Vol 27 (10) ◽  
pp. 1172-1175 ◽  
Author(s):  
Naoki Higashi ◽  
Hirohumi Shoun ◽  
Keiji Yano ◽  
Κει Arima ◽  
Keitaro Hiromi
Keyword(s):  
Complex Formation ◽  
Reduction Rate ◽  
Kinetic Studies ◽  
Stopped Flow ◽  
Apparent Velocity ◽  
Substrate Complex ◽  
Enzyme Substrate ◽  
Hydroxybenzoate Hydroxylase ◽  
Anaerobic Reduction

The spectrophotometric and spectrofluorometric investigations of the enzyme-substrate complex formation of p-hydroxybenzoate hydroxylase was made by the stopped-flow technique. The apparent velocity of the formation of the enzyme-substrate complex (the velocity of the absorbance change in visible and UV regions, and the velocity of the quenching of the fluorescence intensity in the FAD moiety of the holoenzyme by the substrate) was rapid enough to explain the maximal overall velocity (72 sec-1) or the activated anaerobic reduction rate (kredmax= 200 sec-1). The results were consistent with a two-step mechanism involving a rapid bimolecular association of enzyme and substrate, and a slower follow-up unimolecular process.

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