The noncatalytic site-deficient alpha3beta3gamma subcomplex and FoF1-ATP synthase can continuously catalyse ATP hydrolysis when Pi is present.
We investigated ATP hydrolysis by a mutant (DeltaNC) alpha3beta3gamma subcomplex of F0F1-ATP synthase from the thermophilic Bacillus PS3 that is defective in the noncatalytic nucleotide binding sites. This mutant subcomplex was activated by inorganic phosphate ions (Pi) and did not show continuous ATP hydrolysis activity in the absence of Pi. Pi also activated the wild-type alpha3beta3gamma subcomplex in a similar manner. Sulphate activated wild-type alpha3beta3gamma but not DeltaNC alpha3beta3gamma, indicating that Pi activation did not involve noncatalytic sites but that sulphate activation did. Pi also activated ATP hydrolysis and coupled proton translocation by the wild-type and DeltaNC F0F1-ATP synthases reconstituted into vesicle membranes.
Bald
D
D
Tokyo Institute of Technology, Research Laboratory for Resources Utilization, Midori-ku, Yokohama, Japan.
Muneyuki
E
E
Amano
T
T
Kruip
J
J
Hisabori
T
T
Yoshida
M
M
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D004789:Enzyme Activation; D006868:Hydrolysis; D007700:Kinetics; D010710:Phosphates / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011817:Rabbits
D010710:Phosphates; D000255:Adenosine Triphosphate; D006180:Proton-Translocating ATPases