Kinetic and Thermodynamic Analysis of a Physiologic Intermolecular Electron-Transfer Reaction between Methylamine Dehydrogenase and Amicyanin

Biochemistry ◽  
1994 ◽  
Vol 33 (19) ◽  
pp. 5696-5701 ◽  
Author(s):  
Harold B. Brooks ◽  
Victor L. Davidson

1993 ◽  
Vol 294 (1) ◽  
pp. 211-213 ◽  
Author(s):  
H B Brooks ◽  
V L Davidson

The most commonly used methods for analysis of stopped-flow kinetic data require performing a series of measurements in which one reactant is varied at concentrations significantly greater than the concentration of the other reactant. For enzyme-catalysed reactions this may not be possible, because the dissociation constants for the enzyme-substrate complex are often of the same order of magnitude as the high concentrations of enzyme that must frequently be used in stopped-flow studies. An alternative method of data analysis is presented which allows the determination of microscopic rate constants from initial rates of stopped-flow kinetic data in which substrate is varied in a range of concentrations approximately the same as the enzyme. This method also provides a simple and accurate method for determining k4, the rate of the reverse reaction. This method has been used to describe a physiological electron transfer reaction between a quinoprotein, methylamine dehydrogenase, and a copper protein, amicyanin. At 20 degrees C, the rate of the electron-transfer reaction from methylamine dehydrogenase to amicyanin was 24 s-1, and the dissociation constant for complex-formation was 1.9 microM.



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pp. 53374-53378 ◽  
Author(s):  
Kunishige Kataoka ◽  
Kazuya Yamaguchi ◽  
Mayuko Kobayashi ◽  
Tatsuya Mori ◽  
Nobuyuki Bokui ◽  
...  


2011 ◽  
Vol 115 (7) ◽  
pp. 1638-1651 ◽  
Author(s):  
Manoj Kumbhakar ◽  
Swayandipta Dey ◽  
Prabhat Kumar Singh ◽  
Sukhendu Nath ◽  
Ashis Kumar Satpati ◽  
...  








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