Differential detergent solubility investigation of thermally induced transitions in cytochrome c oxidase

Biochemistry ◽  
1987 ◽  
Vol 26 (14) ◽  
pp. 4366-4371 ◽  
Author(s):  
Christopher W. Rigell ◽  
Ernesto Freire
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
Thermally Induced

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.

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