Alpha 3 beta 3 complex of thermophilic ATP synthase. Catalysis without the gamma-subunit.
A complex of the alpha- and beta-subunits of thermophilic ATP synthase showed about 25% of the ATPase activity of the alpha beta gamma complex. The alpha 3 beta 3 hexamer structure was analyzed by sedimentation (11.2 S) and gel filtration (310 kDa). Dilution of the alpha beta complex caused dissociation of the complex and rapid loss of ATPase activity which was restored by addition of the gamma-subunit. A previous method using urea for isolating the subunits resulted in an alpha beta complex with lower activity than that prepared by over-expression of the genes. The alpha beta-ATP complex was formed from the alpha beta complex, ADP and Pi in the presence of dimethyl sulfoxide.
Kagawa
Y
Y
Department of Biochemistry, Jichi Medical School, Tochigi-ken, Japan.
Ohta
S
S
Otawara-Hamamoto
Y
Y
D001419:Bacteria / Q000201:enzymology*; D002384:Catalysis; D002850:Chromatography, Gel; D015394:Molecular Structure; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors / Q000302:isolation & purification*; D013329:Structure-Activity Relationship
D006180:Proton-Translocating ATPases