scholarly journals Cold induced changes of adenosine levels in common eelpout (Zoarces viviparus): a role in modulating cytochrome c oxidase expression

2008 ◽  
Vol 211 (8) ◽  
pp. 1262-1269 ◽  
Author(s):  
L. G. Eckerle ◽  
M. Lucassen ◽  
T. Hirse ◽  
H. O. Portner
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Zoarces Viviparus ◽  
Induced Changes

Thermally induced changes in reconstituted and membranous cytochrome c oxidase

1979 ◽  
Vol 57 (3) ◽  
pp. 238-249 ◽  
Author(s):  
A. S. Denes ◽  
N. Z. Stanacev
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Spin Label ◽  
Liquid Crystalline ◽  
Spectral Characteristics ◽  
Temperature Dependent ◽  
Scanning Calorimetry ◽  
Thermally Induced ◽  
Lipid Protein Interaction ◽  
Induced Changes

The Arrhenius plots of electron transport activity in cytochrome c oxidase reconstituted with well-defined phospholipids have been shown to display a change in slope at 20–25 °C regardless of the chemical nature of the incorporated lipid. In native membranous cytochrome c oxidase, the discontinuity in Arrhenius activity plot occurred at 16–18 °C. These temperature breaks were found to correlate with changes in spin-label mobilities but not with the bulk lipid transition observed by differential scanning calorimetry. Temperature-dependent reciprocal equilibrium between the immobilized and fluid pools is demonstrated. It is suggested that the changes in kinetic and spin-label spectral characteristics in cytochrome c oxidase membranes are related very likely to a lipid-protein interaction prompted by a thermally induced change in the physical state of the lipids that does not involve a gel to liquid crystalline transition.

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.

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