Mutation of αPhe55 of Methylamine Dehydrogenase Alters the Reorganization Energy and Electronic Coupling for Its Electron Transfer Reaction with Amicyanin†,‡

Biochemistry ◽  
2002 ◽  
Vol 41 (47) ◽  
pp. 13926-13933 ◽  
Author(s):  
Dapeng Sun ◽  
Zhi-wei Chen ◽  
F. Scott Mathews ◽  
Victor L. Davidson
Keyword(s):  
Electron Transfer ◽  
Transfer Reaction ◽  
Reorganization Energy ◽  
Electron Transfer Reaction ◽  
Electronic Coupling ◽  
Methylamine Dehydrogenase

scholarly journals A method for extracting rate constants from initial rates of stopped-flow kinetic data: application to a physiological electron-transfer reaction

1993 ◽  
Vol 294 (1) ◽  
pp. 211-213 ◽  
Author(s):  
H B Brooks ◽  
V L Davidson
Keyword(s):  
Electron Transfer ◽  
Rate Constants ◽  
Kinetic Data ◽  
Transfer Reaction ◽  
Dissociation Constants ◽  
Accurate Method ◽  
Electron Transfer Reaction ◽  
Stopped Flow ◽  
Methylamine Dehydrogenase ◽  
Substrate Complex

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.

Nonperturbative Calculation of Electronic Coupling for Electron Transfer Reaction in Proteins

1995 ◽  
Vol 99 (10) ◽  
pp. 2946-2948 ◽  
Author(s):  
Akira Okada ◽  
Toshiaki Kakitani ◽  
Junichiro Inoue
Keyword(s):  
Electron Transfer ◽  
Transfer Reaction ◽  
Electron Transfer Reaction ◽  
Electronic Coupling ◽  
Nonperturbative Calculation

Semiclassical and quantum-mechanical study of the reaction mechanism for the N2 + N2+ electron transfer system

2003 ◽  
Vol 81 (2) ◽  
pp. 125-132
Author(s):  
Yu-Mei Xing ◽  
Lan Chen ◽  
Chong Zhang ◽  
Zun-Sheng Cai ◽  
Xue-Zhuang Zhao
Keyword(s):  
Electron Transfer ◽  
Matrix Element ◽  
Transfer Reaction ◽  
Electron Transfer Reaction ◽  
Transmission Factor ◽  
Quantum Mechanical ◽  
Electronic Coupling ◽  
Transfer System ◽  
Coupling Matrix ◽  
Electron Transfer System

Density functional theory (DFT) calculations, including electron correlation, were carried out on the N2 + N2+ electron transfer system. Six geometries of the precursor complex were assumed and their stabilities were calculated and compared. The activation energy, the electronic transmission factor, and the electronic coupling matrix element in the electron transfer process were also calculated. The electronic transmission factor for this system was far less than unity (ca. 0.006~0.09); thus, the electron transfer reaction was considered to be diabatic in nature. Therefore, the electron transfer rate for the selected structures was calculated using semiclassical and quantum-mechanical theories. The calculated values were compared with each other and were in good agreement with the experimental value.Key words: N2 + N2+ electron transfer reaction, semiclassical and quantum-mechanical theories, electronic transmission factor, electronic coupling matrix element, B3LYP.

scholarly journals A Sphere-Interface Model for the Solvent Reorganization Energy in an Electron Transfer Reaction at the Solvent/Conductor Interface

2009 ◽  
Vol 25 (01) ◽  
pp. 1-5 ◽  
Author(s):  
TU Zhe-Yan ◽  
◽  
LI Xiang-Yuan ◽  
FU Ke-Xiang ◽  
HE Fu-Cheng
Keyword(s):  
Electron Transfer ◽  
Transfer Reaction ◽  
Reorganization Energy ◽  
Electron Transfer Reaction ◽  
Interface Model ◽  
Solvent Reorganization Energy
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