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Single-turnover kinetic experiments confirm the existence of high- and low-affinity ATPase sites in Escherichia coli Lon proteaseTwo ATPasesStructural and functional characterization of a noncanonical nucleoside triphosphate pyrophosphatase fromThermotoga maritimaNovel features of the rotary catalytic mechanism revealed in the structure of yeast F1 ATPase.Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysisHigh-resolution single-molecule characterization of the enzymatic states in Escherichia coli F1-ATPaseAnatomy of F1-ATPase powered rotationChemomechanical coupling in F1-ATPase revealed by simultaneous observation of nucleotide kinetics and rotation.One rotary mechanism for F1-ATPase over ATP concentrations from millimolar down to nanomolarTemperature dependence of the rotation and hydrolysis activities of F1-ATPaseRapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sitesA research journey with ATP synthase.ATP synthesis driven by proton transport in F1F0-ATP synthase.Catalytic site occupancy during ATP synthase catalysis.The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer.Studies of nucleotide binding to the catalytic sites of Escherichia coli betaY331W-F1-ATPase using fluorescence quenching.Identification of the betaTP site in the x-ray structure of F1-ATPase as the high-affinity catalytic site.A functionally important hydrogen-bonding network at the betaDP/alphaDP interface of ATP synthase.Pharmacogenetic significance of inosine triphosphatase.ITPA (inosine triphosphate pyrophosphatase): from surveillance of nucleotide pools to human disease and pharmacogeneticsA more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase.Stepping rotation of F(1)-ATPase with one, two, or three altered catalytic sites that bind ATP only slowly.The new unified theory of ATP synthesis/hydrolysis and muscle contraction, its manifold fundamental consequences and mechanistic implications and its applications in health and disease.Does F1-ATPase have a catalytic site that preferentially binds MgADP?The Escherichia coli F1F0 ATP synthase displays biphasic synthesis kinetics.The binding mechanism of the yeast F1-ATPase inhibitory peptide: role of catalytic intermediates and enzyme turnover.Active site occupancy required for catalytic cooperativity by Escherichia coli transcription termination factor Rho.
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
2001年學術文章
@zh-hant
name
Bi-site catalysis in F1-ATPase: does it exist?
@en
Bi-site catalysis in F1-ATPase: does it exist?
@nl
type
label
Bi-site catalysis in F1-ATPase: does it exist?
@en
Bi-site catalysis in F1-ATPase: does it exist?
@nl
prefLabel
Bi-site catalysis in F1-ATPase: does it exist?
@en
Bi-site catalysis in F1-ATPase: does it exist?
@nl
P2860
P356
P1476
Bi-site catalysis in F1-ATPase: does it exist?
@en
P2093
P2860
P304
35422-35428
P356
10.1074/JBC.M104946200
P407
P577
2001-07-12T00:00:00Z