Biological nano motor, ATP synthase F(o)F(1): from catalysis to gammaepsilonc(10-12) subunit assembly rotation (Q34044494)

30 July 2017

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title

Biological nano motor, ATP synthase F(o)F(1): from catalysis to gammaepsilonc(10-12) subunit assembly rotation (English)

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30 July 2017

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Y Wada

1

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30 July 2017

Y Sambongi

series ordinal

2

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30 July 2017

M Futai

series ordinal

3

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30 July 2017

language of work or name

English

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publication date

1 August 2000

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Biochimica et Biophysica Acta

30 July 2017

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30 July 2017

1459

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30 July 2017

499-505

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30 July 2017

2-3

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ATP synthase (H+-ATPase): results by combined biochemical and molecular biological approaches

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The ATP synthase--a splendid molecular machine

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

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Beta-subunit of Escherichia coli F1-ATPase. An amino acid replacement within a conserved sequence (G-X-X-X-X-G-K-T/S) of nucleotide-binding proteins

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Conserved Glu-181 and Arg-182 residues of Escherichia coli H(+)-ATPase (ATP synthase) beta subunit are essential for catalysis: properties of 33 mutants between beta Glu-161 and beta Lys-201 residues

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Escherichia coli ATP synthase alpha subunit Arg-376: the catalytic site arginine does not participate in the hydrolysis/synthesis reaction but is required for promotion to the steady state

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Mutational replacements of conserved amino acid residues in the alpha subunit change the catalytic properties of Escherichia coli F1-ATPase.

7 January 2021

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Beta subunit Glu-185 of Escherichia coli H(+)-ATPase (ATP synthase) is an essential residue for cooperative catalysis.

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Role of the carboxyl terminal region of H+-ATPase (F0F1a subunit from Escherichia coli

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ATP synthase: an electrochemical transducer with rotatory mechanics

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F0 complex of the Escherichia coli ATP synthase. Not all monomers of the subunit c oligomer are involved in F1 interaction

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Molecular imaging of Escherichia coli F0F1-ATPase in reconstituted membranes using atomic force microscopy

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Topographical structure of membrane-bound Escherichia coli F1F0 ATP synthase in aqueous buffer

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Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase

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Molecular architecture of the rotary motor in ATP synthase

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Beta-gamma subunit interaction is required for catalysis by H(+)-ATPase (ATP synthase). Beta subunit amino acid replacements suppress a gamma subunit mutation having a long unrelated carboxyl terminus

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The ATP synthase gamma subunit. Suppressor mutagenesis reveals three helical regions involved in energy coupling

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

7 January 2021

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Intersubunit rotation in active F-ATPase

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Direct observation of the rotation of F1-ATPase

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The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli

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Electron microscopic evidence of two stalks linking the F1 and F0 parts of the Escherichia coli ATP synthase.

7 January 2021

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Introduction of reactive cysteine residues in the epsilon subunit of Escherichia coli F1 ATPase, modification of these sites with tetrafluorophenyl azide-maleimides, and examination of changes in the binding of the epsilon subunit when different nuc

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Subunits coupling H+ transport and ATP synthesis in the Escherichia coli ATP synthase. Cys-Cys cross-linking of F1 subunit epsilon to the polar loop of F0 subunit c.

7 January 2021

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Characterization of the interface between gamma and epsilon subunits of Escherichia coli F1-ATPase

7 January 2021

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The stalk region of the Escherichia coli ATP synthase. Tyrosine 205 of the gamma subunit is in the interface between the F1 and F0 parts and can interact with both the epsilon and c oligomer.

7 January 2021

1 reference

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Interactions between the F1 and F0 parts in the Escherichia coli ATP synthase. Associations involving the loop region of C subunits.

7 January 2021

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Nucleotide-dependent movement of the epsilon subunit between alpha and beta subunits in the Escherichia coli F1F0-type ATPase

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Disulfide bond formation between the COOH-terminal domain of the beta subunits and the gamma and epsilon subunits of the Escherichia coli F1-ATPase. Structural implications and functional consequences.

7 January 2021

1 reference

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

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Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation

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F-ATPase: specific observation of the rotating c subunit oligomer of EF(o)EF(1)

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Energy transduction in ATP synthase

7 January 2021

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Structural changes linked to proton translocation by subunit c of the ATP synthase

7 January 2021

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10.1016/S0005-2728(00)00189-4

7 January 2021

Identifiers

DOI

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30 July 2017

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