ISSN:
1573-6881
Keywords:
ATP synthase
;
F1
;
oligomer
;
protomer
;
molecular dynamics
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Physics
Notes:
Abstract The basic structures of the catalytic portion (F1, α3β3γδε) of ATP synthase are the α3β3 hexamer (oligomer with cooperativity) and α1β1 heterodimer (protomer). These were reconstituted from the α and β subunits of thermophilic F1 (TF1), and the α3β3 hexamer was crystallized. On electrophoresis, both the dimer and hexamer showed bands with ATPase activity. Using the dimer and hexamer, we studied the nucleotide-dependent rapid molecular dynamics. The formation of the hexamer required neither nucleotide nor Mg. The hexamer was dissociated into the dimer in the presence of MgADP, while the dimer was associated into the hexamer in the presence of MgATP. The hexamer, like mitochondrial F1 and TF1, showed two kinds of ATPase activity: one was cooperative and was inhibited by only one BzADP per hexamer, and the other was inhibited by three BzADP per hexamer.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00762360
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