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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


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



ISSN/ISBN: 0006-2960

DOI: 10.1021/bi026243g


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(PDF emailed within 0-6 h: $19.90)

Accession: 067188699

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Related references

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 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 Journal of Biological Chemistry 271: 818-24, 1996

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

Covalent modification of the catalytic sites of the H(+)-ATPase from chloroplasts, CF(0)F(1), with 2-azido-[alpha-(32)P]ADP: modification of the catalytic site 2 (loose) and the catalytic site 3 (open) impairs multi-site, but not uni-site catalysis of both ATP synthesis and ATP hydrolysis. Biochimica et Biophysica Acta 1456(2-3): 77-98, 2000

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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 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 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

Blocking one non-catalytic ADP binding site results in complete inhibition of the F-type ATPase from the thermophilic Bacillus PS3. Biochimica Et Biophysica Acta 1275(3): 141-144, 1996

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Covalent modification of the catalytic sites of the H+-ATPase from chloroplasts and 2-nitreno-ADP. Modification of the catalytic site 1 (tight) and catalytic sites 1 and 2 together impairs both uni-site and multi-site catalysis of ATP synthesis and ATP hydrolysis. Biochimica et Biophysica Acta 1459(1): 202-217, 2000

Covalent modification of the catalytic sites of the H(+)-ATPase from chloroplasts with 2-nitreno-ADP. Modification of the catalytic site 1 (tight) and catalytic sites 1 and 2 together impairs both uni-site and multi-site catalysis of ATP synthesis and ATP hydrolysis. Biochimica et Biophysica Acta 1459(1): 202-217, 2000

Catalytic site cooperativity of beef heart mitochondrial f 1 atpase correlations of initial velocity bound intermediate and oxygen exchange measurements with an alternating 3 site model. Journal of Biological Chemistry 257(20): 12030-12038, 1982