The a3b3c subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 with the bT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover

The alpha3beta3gamma subcomplex of the F1-ATPase from the thermophilic bacillus PS3 with the betaT165S substitution does not entrap inhibitory MgADP in a catalytic site during turnover. Journal of Biological Chemistry 271(46): 28818-28824, 1996

The a3b3c complex of the F1-ATPase from thermophilic Bacillus PS3 containing the aD261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites. Biochemistry (American Chemical Society) 34: 412-18, 1995

The Characteristics of the (aV371C)3(bR337C)3g Double Mutant Subcomplex of the TF1-ATPase Indicate that the Catalytic Site at the aTP-bTP Interface with Bound MgADP in Crystal Structures of MF1 Represents a Catalytic Site Containing Inhibitory MgADP. Biochemistry (American Chemical Society) 44(7): 41-8, 2005

The alpha 3 beta 3 gamma complex of the F1-ATPase from thermophilic Bacillus PS3 containing the alpha D261N substitution fails to dissociate inhibitory MgADP from a catalytic site when ATP binds to noncatalytic sites. Biochemistry 34(50): 16412-16418, 1995

The characteristics of the (alpha V371C)3(beta R337C)3 gamma double mutant subcomplex of the TF1-ATPase indicate that the catalytic site at the alpha TP-beta TP interface with bound MgADP in crystal structures of MF1 represents a catalytic site containing inhibitory MgADP. Biochemistry 44(7): 2441-2448, 2005

Characteristics of protection by MgADP and MgATP of α3β3γ subcomplex of thermophilic Bacillus PS3 βY341W-mutant F1-ATPase from inhibition by 7-chloro-4-nitrobenz-2-oxa-1,3-diazole support a bi-site mechanism of catalysis. Biochemistry. Biokhimiia 76(11): 1253-1261, 2011

Substitution of b-Glu201 in the a3b3c subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides. The Journal of Biological Chemistry 275(14): 057-63, 2000

Substitution of betaGlu(201) in the alpha(3)beta(3)gamma subcomplex of the F(1)-ATPase from the thermophilic Bacillus PS3 increases the affinity of catalytic sites for nucleotides. Journal of Biological Chemistry 275(14): 10057-10063, 2000

The G 156 C Substitution in the F 1 -Atpase from the Thermophilic Bacillus Ps3 Affects Catalytic Site Cooperativity by Destabilizing the Closed Conformation of the Catalytic Site. Biochemistry 41(48): 14421-14429, 2002

The bG156C Substitution in the F1-ATPase from the Thermophilic Bacillus PS3 Affects Catalytic Site Cooperativity by Destabilizing the Closed Conformation of the Catalytic Site. Biochemistry (American Chemical Society) 41(48): 421-9, 2002

The beta G156C substitution in the F1-ATPase from the thermophilic Bacillus PS3 affects catalytic site cooperativity by destabilizing the closed conformation of the catalytic site. Biochemistry 41(48): 14421-14429, 2002

The a3(bY341W)3c subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP. Biochemistry (American Chemical Society) 37(47): 757-64, 1998

The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgATP. Biochemistry 37(47): 16757-16764, 1998

The (aF357C)3(bR372C)3c subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 altered ATPase activity after cross-linking a and b subunits at noncatalytic site interfaces. Biochemistry (American Chemical Society) 41(9): 26-34, 2002

Lowered temperature or binding of pyrophosphate to sites for noncatalytic nucleotides modulates the ATPase activity of the beef heart mitochondrial F1-ATPase by decreasing the affinity of a catalytic site for inhibitory MgADP. Biochemistry 33(50): 14979-14985, 1994