Adsorption Orientation of Horse Heart Cytochrome c on a Bare Gold Electrode Hampers Its Electron Transfer

2011 ◽  
Vol 116 (1) ◽  
pp. 637-642 ◽  
Author(s):  
Shourui Lin ◽  
Xiue Jiang ◽  
Lixu Wang ◽  
Guihua Li ◽  
Liping Guo
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Gold Electrode ◽  
Horse Heart Cytochrome ◽  
Bare Gold Electrode ◽  
Horse Heart Cytochrome C ◽  
Bare Gold

High-driving-force electron transfer in horse heart cytochrome C.

1991 ◽  
Vol 43 (2-3) ◽  
pp. 104
Author(s):  
I-Jy Chang ◽  
Jay R. Winkler ◽  
Harry B. Gray
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Driving Force ◽  
Horse Heart Cytochrome ◽  
Horse Heart Cytochrome C

scholarly journals Kinetics of carbon monoxide binding and electron transfer by cytochrome c polymers

1974 ◽  
Vol 141 (1) ◽  
pp. 299-304 ◽  
Author(s):  
Silvestro Dupré ◽  
Maurizio Brunori ◽  
Michael T. Wilson ◽  
Colin Greenwood
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Unique Type ◽  
Horse Heart Cytochrome ◽  
Methionine Residue ◽  
Titration Data ◽  
Carbon Monoxide Binding ◽  
Horse Heart Cytochrome C ◽  
Kinetics Of ◽  
Recombination Kinetics

Studies on horse heart cytochrome c polymers were carried out by stopped-flow and photolysis techniques, to investigate the properties of the CO complex and the kinetics of electron transfer, mainly of the dimeric and tetrameric forms. CO binding, which does not occur with native monomers, proceeds at both pH7.0 and pH9.6, and appears to follow complex kinetics: an initial phase is observed, which is CO-concentration-dependent, followed by a very slow monomolecular phase (k~2×10-3s-1 at pH7) before establishment of equilibrium. Photodissociation of the CO complex has a very low quantum yield, probably less than 0.1. Static titration data of the dimer gave an ‘n’ value of 0.4. These data strongly suggest heterogeneity of the population of binding sites, and have been interpreted in terms of the existence of different structures, probably owing to the non-unique type of binding of monomers during polymerization. Polymers of cytochrome c carboxymethylated on the methionine residue normally ligated to iron show simple CO recombination kinetics after photolytic removal (kon=1.5×106m-1·s-1 at pH6). We therefore suggest that, for native cytochrome c, polymerization has an effect on the lability of the haem crevice, rendering the iron available for binding ligands, without, however, forming the structure of a truly open crevice. Electron transfer is, on the other hand, a simple process, and no gross differences are observed between monomer and polymers. A simple model, taking into account all these data, is suggested.

722—The effect of pH on the temperature dependence of the redox potential of horse heart cytochrome c at a bis(4-pyridyl)disulfide-modified gold electrode

1984 ◽  
Vol 13 (4-6) ◽  
pp. 373-383 ◽  
Author(s):  
Isao Taniguchi ◽  
Masahiro Iseki ◽  
Takaki Eto ◽  
Kenji Toyosawa ◽  
Hiroko Yamaguchi ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Redox Potential ◽  
Temperature Dependence ◽  
Gold Electrode ◽  
Horse Heart Cytochrome ◽  
Effect Of Ph ◽  
Horse Heart Cytochrome C

Ruthenium-modified horse heart cytochrome c: effect of pH and ligation on the rate of intramolecular electron transfer between ruthenium(II) and heme(III)

1986 ◽  
Vol 90 (16) ◽  
pp. 3800-3804 ◽  
Author(s):  
Rolf Bechtold ◽  
Mary B. Gardineer ◽  
Arif Kazmi ◽  
Bruno Van Hemelryck ◽  
Stephan S. Isied
Keyword(s):  
Electron Transfer ◽  
Cytochrome C ◽  
Intramolecular Electron Transfer ◽  
Horse Heart Cytochrome ◽  
Effect Of Ph ◽  
Horse Heart Cytochrome C

Nanoscopic and Redox Characterization of Engineered Horse Cytochrome c Chemisorbed on a Bare Gold Electrode

2007 ◽  
Vol 26 (4) ◽  
pp. 271-279 ◽  
Author(s):  
Laura Andolfi ◽  
Paola Caroppi ◽  
Anna Rita Bizzarri ◽  
Maria Cristina Piro ◽  
Federica Sinibaldi ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Gold Electrode ◽  
Bare Gold Electrode ◽  
Horse Cytochrome ◽  
Bare Gold
Sign in / Sign up

Export Citation Format

Share Document