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.
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Regulation of the F0F1-ATP synthase: the conformation of subunit epsilon might be determined by directionality of subunit gamma rotationPurine but not pyrimidine nucleotides support rotation of F(1)-ATPase.F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.ATP-driven stepwise rotation of FoF1-ATP synthase.The rotary machine in the cell, ATP synthase.Activation of pausing F1 motor by external forceResolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.Pause and rotation of F(1)-ATPase during catalysisHow azide inhibits ATP hydrolysis by the F-ATPases.ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.A functionally inactive, cold-stabilized form of the Escherichia coli F1Fo ATP synthase.ATP hydrolysis and synthesis of a rotary motor V-ATPase from Thermus thermophilusRegulation of the thermoalkaliphilic F1-ATPase from Caldalkalibacillus thermarumThermophilic F1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit.Molecular processes of inhibition and stimulation of ATP synthase caused by the phytotoxin tentoxin.Oxidation of the alpha(3)(betaD311C/R333C)(3)gamma subcomplex of the thermophilic Bacillus PS3 F(1)-ATPase indicates that only two beta subunits can exist in the closed conformation simultaneously.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.Single-molecule analysis of F0F1-ATP synthase inhibited by N,N-dicyclohexylcarbodiimideRole of the DELSEED loop in torque transmission of F1-ATPase.alpha3beta3gamma complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites.Severe MgADP inhibition of Bacillus subtilis F1-ATPase is not due to the absence of nucleotide binding to the noncatalytic nucleotide binding sites.Complete inhibition and partial Re-activation of single F1-ATPase molecules by tentoxin: new properties of the re-activated enzyme.Regulatory interplay between proton motive force, ADP, phosphate, and subunit epsilon in bacterial ATP synthase.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.Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site.Photoinactivation of the F1-ATPase from spinach chloroplasts by dequalinium is accompanied by derivatization of methionine beta183.Cross-linking of two beta subunits in the closed conformation in F1-ATPase.F1-ATPase changes its conformations upon phosphate release.
P2860
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P2860
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.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh-hant
name
The alpha 3 beta 3 gamma compl ...... P binds to noncatalytic sites.
@en
The alpha 3 beta 3 gamma compl ...... P binds to noncatalytic sites.
@nl
type
label
The alpha 3 beta 3 gamma compl ...... P binds to noncatalytic sites.
@en
The alpha 3 beta 3 gamma compl ...... P binds to noncatalytic sites.
@nl
prefLabel
The alpha 3 beta 3 gamma compl ...... P binds to noncatalytic sites.
@en
The alpha 3 beta 3 gamma compl ...... P binds to noncatalytic sites.
@nl
P2093
P356
P1433
P1476
The alpha 3 beta 3 gamma compl ...... P binds to noncatalytic sites.
@en
P2093
E Muneyuki
W S Allison
P304
16412-16418
P356
10.1021/BI00050A023
P407
P577
1995-12-01T00:00:00Z