Relation of Structural Changes to Electron-Transfer Parameters in Fulvalenediyl Dirhodium Complexes Demonstrating Quasi-Reversible Two-Electron Voltammetry†

1996 ◽  
Vol 118 (21) ◽  
pp. 5002-5010 ◽  
Author(s):  
Teen T. Chin ◽  
William E. Geiger ◽  
Arnold L. Rheingold
Keyword(s):  
Electron Transfer ◽  
Structural Changes ◽  
Transfer Parameters ◽  
Dirhodium Complexes

scholarly journals An examination of how structural changes can affect the rate of electron transfer in a mutated bacterial photoreaction centre

2000 ◽  
Vol 351 (3) ◽  
pp. 567 ◽  
Author(s):  
Justin P. RIDGE ◽  
Paul K. FYFE ◽  
Katherine E. McAULEY ◽  
Marion E. van BREDERODE ◽  
Bruno ROBERT ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Structural Changes

Estimation of Electron Transfer Parameters from AM1 Calculations

2001 ◽  
Vol 66 (20) ◽  
pp. 6551-6559 ◽  
Author(s):  
Stephen F. Nelsen ◽  
Fredrik Blomgren
Keyword(s):  
Electron Transfer ◽  
Am1 Calculations ◽  
Transfer Parameters

Determination of electron transfer parameters via the semiintegral

1973 ◽  
Vol 45 (13) ◽  
pp. 2175-2178 ◽  
Author(s):  
J. H. Carney ◽  
H. C. Miller
Keyword(s):  
Electron Transfer ◽  
Transfer Parameters

scholarly journals Electron-transfer‐mediated binding of optically active cobalt(III) complexes to horse heart cytochrome c

2005 ◽  
Vol 2 (2) ◽  
pp. 109-112 ◽  
Author(s):  
Ulrich Scholten ◽  
Alejandro Castillejo Merchán ◽  
Klaus Bernauer
Keyword(s):  
Electron Transfer ◽  
Structural Changes ◽  
Electron Transfer Reaction ◽  
Optically Active ◽  
Cd Spectra ◽  
Reaction Products ◽  
Horse Heart Cytochrome ◽  
Histidine Residues ◽  
Horse Heart Cytochrome C ◽  
Haem Iron

Optically active cobalt(II) complexes are used as reducing agents in the electron-transfer reaction involving horse heart cytochrome c . Analysis of the circular dichroism (CD) spectra of reaction products indicates that the corresponding cobalt(III) species of both enantiomers of [Co II (alamp)] (H 2 alamp= N , N ′-[(pyridine-2,6-diyl)bis(methylene)]-bis[alanine]) are partly attached to the protein during electron transfer by coordination to an imidazole unit of one of the histidine residues. His-26 and His-33 are both solvent exposed, and the results suggest that one of these histidine residues acts as a bridge in the electron transfer to and from the haem iron of cytochrome c . The reaction is enantioselective: the ratio of the relative reactivity at 15 °C is 2.9 in favour of the R , R -enantiomer. A small induced CD activity in the haem chromophore reveals that some structural changes in the protein occur consecutively with the binding of the cobalt(III) complex.

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