Electron transfer in trimethylamine dehydrogenase and electrontransferring flavoprotein

1999 ◽  
Vol 27 (2) ◽  
pp. 196-201 ◽  
Author(s):  
N. S. Scrutton ◽  
J. Basran ◽  
E. K. Wilson ◽  
K. K. Chohan ◽  
M.-H. Jang ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Trimethylamine Dehydrogenase

Flavin radicals, conformational sampling and robust design principles in interprotein electron transfer: the trimethylamine dehydrogenase-electron-transferring flavoprotein complex

2004 ◽  
Vol 71 ◽  
pp. 1-14
Author(s):  
David Leys ◽  
Jaswir Basran ◽  
François Talfournier ◽  
Kamaldeep K. Chohan ◽  
Andrew W. Munro ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Dimensional Space ◽  
Three Dimensional ◽  
Kinetic Studies ◽  
Molecular Assembly ◽  
Conformational Sampling ◽  
Trimethylamine Dehydrogenase ◽  
Key Residues ◽  
Electron Transferring Flavoprotein ◽  
Electron Transfer Complex

TMADH (trimethylamine dehydrogenase) is a complex iron-sulphur flavoprotein that forms a soluble electron-transfer complex with ETF (electron-transferring flavoprotein). The mechanism of electron transfer between TMADH and ETF has been studied using stopped-flow kinetic and mutagenesis methods, and more recently by X-ray crystallography. Potentiometric methods have also been used to identify key residues involved in the stabilization of the flavin radical semiquinone species in ETF. These studies have demonstrated a key role for 'conformational sampling' in the electron-transfer complex, facilitated by two-site contact of ETF with TMADH. Exploration of three-dimensional space in the complex allows the FAD of ETF to find conformations compatible with enhanced electronic coupling with the 4Fe-4S centre of TMADH. This mechanism of electron transfer provides for a more robust and accessible design principle for interprotein electron transfer compared with simpler models that invoke the collision of redox partners followed by electron transfer. The structure of the TMADH-ETF complex confirms the role of key residues in electron transfer and molecular assembly, originally suggested from detailed kinetic studies in wild-type and mutant complexes, and from molecular modelling.

Stepwise electron transfer to 6-S cysteinyl FMN in trimethylamine dehydrogenase

1999 ◽  
Vol 27 (1) ◽  
pp. A45-A45
Author(s):  
J. Basran ◽  
M-H. Jang ◽  
M. J. Sutcliffe ◽  
R. Hille ◽  
N. S. Scrutton
Keyword(s):  
Electron Transfer ◽  
Trimethylamine Dehydrogenase

scholarly journals Electron Transfer and Conformational Change in Complexes of Trimethylamine Dehydrogenase and Electron Transferring Flavoprotein

2001 ◽  
Vol 277 (10) ◽  
pp. 8457-8465 ◽  
Author(s):  
Matthew Jones ◽  
Francois Talfournier ◽  
Anton Bobrov ◽  
J. Günter Grossmann ◽  
Nikolai Vekshin ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Conformational Change ◽  
Trimethylamine Dehydrogenase ◽  
Electron Transferring Flavoprotein
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