Spectroscopic and Kinetic Studies of the Tetraheme Flavocytochrome c From Shewanella putrefaciens NCIMB400

Biochemistry ◽  
1995 ◽  
Vol 34 (18) ◽  
pp. 6153-6158 ◽  
Author(s):  
Sara L. Pealing ◽  
Myles R. Cheesman ◽  
Graeme A. Reid ◽  
Andrew J. Thomson ◽  
F. Bruce Ward ◽  
...  
Keyword(s):  
Kinetic Studies ◽  
Shewanella Putrefaciens ◽  
Flavocytochrome C

Flavocytochrome c: A soluble fumarate reductase from Shewanella putrefaciens.

1993 ◽  
Vol 51 (1-2) ◽  
pp. 183
Author(s):  
Sara L Pealing ◽  
Ann C Black ◽  
Myles R Cheesman ◽  
Stephen K Chapman ◽  
F Bruce Ward ◽  
...  
Keyword(s):  
Shewanella Putrefaciens ◽  
Fumarate Reductase ◽  
Flavocytochrome C

Electrochemical Properties of pH-Dependent Flavocytochrome C 3 from Shewanella Putrefaciens Adsorbed Onto Catechol-Modified Carbon Electrode

2020 ◽  
Vol MA2020-01 (44) ◽  
pp. 2522-2522
Author(s):  
Estelle Lebègue ◽  
Nazua L Costa ◽  
Bruno M Fonseca ◽  
Ricardo O Louro ◽  
Frédéric Barrière
Keyword(s):  
Electrochemical Properties ◽  
Shewanella Putrefaciens ◽  
Carbon Electrode ◽  
Flavocytochrome C ◽  
Ph Dependent

Flavocytochrome C - a novel fumarate reductase from Shewanella putrefaciens

1991 ◽  
Vol 43 (2-3) ◽  
pp. 311 ◽  
Author(s):  
S.L. Pealing ◽  
A.C. Black ◽  
S.K. Chapman ◽  
F.B. Ward ◽  
G.A. Reid
Keyword(s):  
Shewanella Putrefaciens ◽  
Fumarate Reductase ◽  
Flavocytochrome C

Expression of flavocytochrome C from Shewanella putrefaciens

1993 ◽  
Vol 51 (1-2) ◽  
pp. 589 ◽  
Author(s):  
F.D.C. Manson ◽  
S.L. Pealing ◽  
F.B. Ward ◽  
S.K. Chapman ◽  
G.A. Reid
Keyword(s):  
Shewanella Putrefaciens ◽  
Flavocytochrome C

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.

Sign in / Sign up

Export Citation Format

Share Document