Temperature‐dependent conformational changes in isolated oligomycin‐sensitive ATPase

Abstract
Isolated oligomycin-sensitive ATPase undergoes a kinetic change at 20–25°C with a higher activation energy and a lower K m for ATP below this temperature range. This observation has been correlated with temperature-dependent structural changes detected by circular dichroism in the UV region in the isolated enzyme. The negative ellipticities in the 208-225 nm region, which are proportional to the α-helix content, increase with rise in temperature to a maximum above 25°C.