Expression of the wild-type and the Cys-/Trp-less alpha 3 beta 3 gamma complex of thermophilic F1-ATPase in Escherichia coli.
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Filming biomolecular processes by high-speed atomic force microscopyPurine but not pyrimidine nucleotides support rotation of F(1)-ATPase.Direct observation of the rotation of epsilon subunit in F1-ATPase.The rotary machine in the cell, ATP synthase.Pause and rotation of F(1)-ATPase during catalysisCatalysis and rotation of F1 motor: cleavage of ATP at the catalytic site occurs in 1 ms before 40 degree substep rotationThe rotor tip inside a bearing of a thermophilic F1-ATPase is dispensable for torque generation.ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.The beta subunit loop that couples catalysis and rotation in ATP synthase has a critical length.Winding single-molecule double-stranded DNA on a nanometer-sized reel.The role of the betaDELSEED-loop of ATP synthase.The chloroplast ATP synthase features the characteristic redox regulation machinery.Stepping rotation of F(1)-ATPase with one, two, or three altered catalytic sites that bind ATP only slowly.Substitution of a single amino acid switches the tentoxin-resistant thermophilic F1-ATPase into a tentoxin-sensitive enzyme.Thermophilic F1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit.A conformational change of the γ subunit indirectly regulates the activity of cyanobacterial F1-ATPase.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.Expression of mammalian mitochondrial F1-ATPase in Escherichia coli depends on two chaperone factors, AF1 and AF2.Inverse regulation of F1-ATPase activity by a mutation at the regulatory region on the gamma subunit of chloroplast ATP synthasealpha3beta3gamma complex of F1-ATPase from thermophilic Bacillus PS3 can maintain steady-state ATP hydrolysis activity depending on the number of non-catalytic sites.Thermodynamic analyses of nucleotide binding to an isolated monomeric β subunit and the α3β3γ subcomplex of F1-ATPaseTorque generation in F1-ATPase devoid of the entire amino-terminal helix of the rotor that fills half of the stator orifice.Neither helix in the coiled coil region of the axle of F1-ATPase plays a significant role in torque production.Complete inhibition and partial Re-activation of single F1-ATPase molecules by tentoxin: new properties of the re-activated enzyme.Role of the epsilon subunit of thermophilic F1-ATPase as a sensor for ATP.Catalytic activities of alpha3beta3gamma complexes of F1-ATPase with 1, 2, or 3 incompetent catalytic sites.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.Unusual pKa of the carboxylate at the putative catalytic position of the thermophilic F1-ATPase beta subunit determined by 13C-NMR.Catalytic activity of the alpha3beta3gamma complex of F1-ATPase without noncatalytic nucleotide binding site.The regulatory functions of the gamma and epsilon subunits from chloroplast CF1 are transferred to the core complex, alpha3beta3, from thermophilic bacterial F1.Cross-linking of two beta subunits in the closed conformation in F1-ATPase.The noncatalytic site-deficient alpha3beta3gamma subcomplex and FoF1-ATP synthase can continuously catalyse ATP hydrolysis when Pi is present.Epsilon subunit, an endogenous inhibitor of bacterial F(1)-ATPase, also inhibits F(0)F(1)-ATPase.ATPase activity of a highly stable alpha(3)beta(3)gamma subcomplex of thermophilic F(1) can be regulated by the introduced regulatory region of gamma subunit of chloroplast F(1).The role of the DELSEED motif of the beta subunit in rotation of F1-ATPase.Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase.The role of the betaDELSEED motif of F1-ATPase: propagation of the inhibitory effect of the epsilon subunit.The fluorescence spectrum of the introduced tryptophans in the alpha 3(beta F155W)3gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 cannot be used to distinguish between the number of nucleoside di- and triphosphates bound to catThe presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F(1)-ATPase.
P2860
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P2860
Expression of the wild-type and the Cys-/Trp-less alpha 3 beta 3 gamma complex of thermophilic F1-ATPase in Escherichia coli.
description
1995 nî lūn-bûn
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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
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1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
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1995年學術文章
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name
Expression of the wild-type an ...... F1-ATPase in Escherichia coli.
@en
Expression of the wild-type an ...... F1-ATPase in Escherichia coli.
@nl
type
label
Expression of the wild-type an ...... F1-ATPase in Escherichia coli.
@en
Expression of the wild-type an ...... F1-ATPase in Escherichia coli.
@nl
prefLabel
Expression of the wild-type an ...... F1-ATPase in Escherichia coli.
@en
Expression of the wild-type an ...... F1-ATPase in Escherichia coli.
@nl
P1476
Expression of the wild-type an ...... F1-ATPase in Escherichia coli.
@en
P2093
P304
P356
10.1016/0005-2728(95)00070-Y
P577
1995-09-01T00:00:00Z