Bi-site catalysis in F1-ATPase: does it exist? (Q43672989)

25 November 2017

title

Bi-site catalysis in F1-ATPase: does it exist? (English)

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25 November 2017

Weber J

1

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25 November 2017

Senior AE

series ordinal

2

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25 November 2017

language of work or name

English

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publication date

12 July 2001

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Journal of Biological Chemistry

25 November 2017

published in

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25 November 2017

volume

276

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25 November 2017

issue

38

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25 November 2017

page(s)

35422-35428

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Catalytic mechanism of F1-ATPase

25 November 2017

cites work

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Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria

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Direct observation of the rotation of F1-ATPase

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Direct observation of the rotation of epsilon subunit in F1-ATPase

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Unisite catalysis without rotation of the gamma-epsilon domain in Escherichia coli F1-ATPase

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The binding change mechanism for ATP synthase--some probabilities and possibilities

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From chemistry to biochemistry to catalysis to movement

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Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase

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Purine but not pyrimidine nucleotides support rotation of F(1)-ATPase.

21 January 2018

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Stability constants of magnesium and cadmium complexes of adenine nucleotides and thionucleotides and rate constants for formation and dissociation of magnesium-ATP and magnesium-ADP

21 January 2018

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The ATP synthase--a splendid molecular machine

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Bi-site activation occurs with the native and nucleotide-depleted mitochondrial F1-ATPase

21 January 2018

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Kinetic mechanism of mitochondrial adenosine triphosphatase. ADP-specific inhibition as revealed by the steady-state kinetics

21 January 2018

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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.

21 January 2018

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Specific tryptophan substitution in catalytic sites of Escherichia coli F1-ATPase allows differentiation between bound substrate ATP and product ADP in steady-state catalysis

21 January 2018

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ATP synthase: what we know about ATP hydrolysis and what we do not know about ATP synthesis

21 January 2018

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The mechanism and regulation of ATP synthesis by F1-ATPases

21 January 2018

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Catalytic site forms and controls in ATP synthase catalysis

21 January 2018

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Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase

21 January 2018

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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

21 January 2018

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21 January 2018

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A nonlinear approach for the analysis of different models of protein-ligand interaction: nucleotide binding to F1-ATPase

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M104946200

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25 November 2017

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