A temperature-dependent structural change of mitochondrial ATPase.
The temperature dependence of the intrinsic tryptophan fluorescence in either bovine heart submitochondrial particles or oligomycin-sensitive ATPase isolated therefrom shows a discontinuity at near 25 degrees C, which coincides with the temperature where a break in the Arrhenius plot of ATPase activity is found. Addition of n-butanol to submitochondrial particles induces a decrease of tryptophan fluorescence in the whole temperature range. The discontinuity is interpreted as a temperature-dependent structural change and related to a viscosity-induced phase separation of the intrinsic mitochondrial proteins.
D020001:1-Butanol; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D000440:Butanols / Q000494:pharmacology; D002417:Cattle; D008929:Mitochondria, Heart / Q000201:enzymology*; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013367:Submitochondrial Particles / Q000201:enzymology; D013696:Temperature
D000440:Butanols; D020001:1-Butanol; D000251:Adenosine Triphosphatases