scholarly journals Studies of the Ruthenium Complexes. XIII. Kinetic Studies of Electrontransfer Reactions between Aquapentaammineruthenium(II) and Halopentaammineruthenium(III) Comlexes

1977 ◽  
Vol 50 (3) ◽  
pp. 666-669 ◽  
Author(s):  
Akira Ohyoshi ◽  
Kenichiro Yoshikuni ◽  
Hidetoshi Ohtsuyama ◽  
Tomohisa Yamashita ◽  
Shigeyoshi Sakaki
Keyword(s):  
Ruthenium Complexes ◽  
Kinetic Studies

scholarly journals Studies on the Ruthenium Complexes. IX. Kinetic Studies on the Deaquation-anation Reaction of Aquapentaammineruthenium(III) Complexes

1975 ◽  
Vol 48 (1) ◽  
pp. 262-265 ◽  
Author(s):  
Akira Ohyoshi ◽  
Shun-ichi Hiraki ◽  
Tomio Odate ◽  
Susumu Kohata ◽  
Junko Oda
Keyword(s):  
Ruthenium Complexes ◽  
Kinetic Studies ◽  
Anation Reaction

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.

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