The Journal of Biochemistry · 1978 · 59 citations · 0 references
Natural SciencesBiochemistryBiophysicsEnzymologyMembrane BiophysicsMolecular BiophysicsAtp HydrolysisMembrane DynamicsProtein DynamicsArrhenius EquationCalcium AtpaseEnzyme Conformational ChangeMembrane AtpasesRotational Correlation TimeRotational DynamicsRotational MotionSarcoplasmic Reticulum Calcium Atpases
The technique of saturation transfer electron spin resonance has been applied to study the rotational diffusion of spin-labeled Ca2+, Mg2+-dependent ATPase molecules in the membranes of sarcoplasmic reticulum vesicles. Comparison of the present data with those for spin-labeled hemoglobin undergoing isotropic rotation leads to a value of 2 X 10(-4) s for the apparent rotational correlation time at 20 degrees C for the membrane-bound protein. Consideration of the anisotropy of the Brownian rotation of the membrane-bound ATPase suggests that the true correlation time for the expected axial rotation may be somewhat smaller than the apparent value. An Arrhenius plot of the rotational motion shows a break, which is interpreted as indicating the occurrence of a conformational change of the ATPase molecule at about 15 degrees C.