scholarly journals Alkaline Isomerization of Ferricytochrome c: Identification of the Lysine Ligand

1974 ◽  
Vol 71 (7) ◽  
pp. 2892-2894 ◽  
Author(s):  
H. Wilgus ◽  
E. Stellwagen
Keyword(s):  
Ferricytochrome C ◽  
Alkaline Isomerization

Time-resolved resonance Raman study of alkaline isomerization of ferricytochrome c

Biochemistry ◽  
1984 ◽  
Vol 23 (26) ◽  
pp. 6802-6808 ◽  
Author(s):  
Tadayuki Uno ◽  
Yoshifumi Nishimura ◽  
Masamichi Tsuboi
Keyword(s):  
Resonance Raman ◽  
Time Resolved ◽  
Ferricytochrome C ◽  
Raman Study ◽  
Alkaline Isomerization

The alkaline isomerization of lysine-modified ferricytochrome c

1975 ◽  
Vol 405 (1) ◽  
pp. 115-121 ◽  
Author(s):  
Earle Stellwagen ◽  
Jorge Babul ◽  
Harvey Wilgus
Keyword(s):  
Ferricytochrome C ◽  
Alkaline Isomerization

scholarly journals 1H-n.m.r. evaluation of the ferricytochrome c-cardiolipin interaction. Effect of superoxide radicals

1990 ◽  
Vol 265 (1) ◽  
pp. 227-232 ◽  
Author(s):  
B Soussi ◽  
A C Bylund-Fellenius ◽  
T Scherstén ◽  
J Ångström
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Native Structure ◽  
Hydrogen Bond Interactions ◽  
Ferrocytochrome C ◽  
Ischaemia And Reperfusion ◽  
Ferricytochrome C ◽  
Induced Changes ◽  
Alkaline Isomerization

The interaction between ferricytochrome c and cardiolipin was investigated by 1H n.m.r. at 270 MHz. From the phospholipid-induced changes of the protein spectral features it is concluded that the first 2 equivalents of cardiolipin cause a conformational change at the lower part of the solvent-exposed haem edge, involving a rearrangement of the hydrogen-bond interactions of propionate 6, thus partly accounting for the lowered redox potential of cytochrome c in the presence of cardiolipin. The increased value for the pK of the alkaline isomerization of ferricytochrome c shows that cardiolipin stabilizes the native structure of the protein, indicating that the oxidized form assumes ferrocytochrome c-like properties. Peroxidation of cardiolipin by superoxide radical ions drastically decreases the protein binding to this phospholipid. The implications of this finding, and the likelihood of the ternary cytochrome c-cardiolipin-cytochrome c oxidase complex, for the binding of cytochrome c to cytochrome c oxidase in vivo, are discussed in relation to peroxidative damage following ischaemia and reperfusion.

scholarly journals Crystallization of tuna ferricytochrome c at low ionic strength.

1990 ◽  
Vol 265 (8) ◽  
pp. 4177-4180
Author(s):  
M H Walter ◽  
E M Westbrook ◽  
S Tykodi ◽  
A M Uhm ◽  
E Margoliash
Keyword(s):  
Ionic Strength ◽  
Ferricytochrome C ◽  
Low Ionic Strength
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