The kinetic and structural changes of the mitochondrial F1-ATPase with temperature.
Mitochondrial F1-ATPase shows a break in the Arrhenius plot with an increase of the activation energy below 17 degrees C, this may imply that the F1-ATPase undergoes a conformational change at this temperature. Further, a structural change of the F1-ATPase is indicated by analysis of the intrinsic fluorescence at 307 nm between 33 and 11 degrees C and also by evaluation of the circular dichroism spectra of the enzyme at temperatures below and above the temperature corresponding to the discontinuity of the Arrhenius plot. It is therefore suggested that F1-ATPase exists in two temperature dependent conformational states to which different catalytic properties may be assigned.
Baracca
A
A
Curatola
G
G
Parenti Castelli
G
G
Solaini
G
G
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D004591:Electrophoresis, Polyacrylamide Gel; D007700:Kinetics; D008929:Mitochondria, Heart / Q000201:enzymology*; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D013696:Temperature
D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases