Conformational transmission in ATP synthase during catalysis: search for large structural changes (Q41252039)

28 September 2017

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title

Conformational transmission in ATP synthase during catalysis: search for large structural changes (English)

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28 September 2017

M Futai

1

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28 September 2017

H Omote

series ordinal

2

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28 September 2017

publication date

1 October 1996

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Journal of Bioenergetics and Biomembranes

28 September 2017

published in

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28 September 2017

volume

28

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28 September 2017

issue

5

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28 September 2017

page(s)

409-414

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Escherichia coli H(+)-ATPase (ATP synthase): catalytic site and roles of subunit interactions in energy coupling.

28 September 2017

cites work

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Crossref

https://api.crossref.org/works/10.1007%2FBF02113982

Further examination of seventeen mutations in Escherichia coli F1-ATPase beta-subunit

21 January 2018

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12 December 2020

The defective proton-ATPase of uncD mutants of Escherichia coli. Two mutations which affect the catalytic mechanism.

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12 December 2020

The specificity of carboxyl group modification during the inactivation of the Escherichia coli F1-ATPase with dicyclohexyl[14C]carbodiimide

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12 December 2020

Replacement of arginine 246 by histidine in the beta subunit of Escherichia coli H+-ATPase resulted in loss of multi-site ATPase activity

1 reference

12 December 2020

H(+)-ATPase gamma subunit of Escherichia coli. Role of the conserved carboxyl-terminal region

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12 December 2020

The proton pore in the Escherichia coli F0F1-ATPase: substitution of glutamate by glutamine at position 219 of the alpha-subunit prevents F0-mediated proton permeability

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12 December 2020

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

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12 December 2020

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

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12 December 2020

Suppression mutations in the defective beta subunit of F1-ATPase from Escherichia coli

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12 December 2020

Replacement of serine 373 by phenylalanine in the alpha subunit of Escherichia coli F1-ATPase results in loss of steady-state catalysis by the enzyme

1 reference

12 December 2020

Catalytic site nucleotide and inorganic phosphate dependence of the conformation of the .epsilon. subunit in the Escherichia coli adenosinetriphosphatase

1 reference

12 December 2020

Localization of sites modified during inactivation of the bovine heart mitochondrial F1-ATPase by quinacrine mustard using [3H]aniline as a probe

1 reference

12 December 2020

Effects of mutations of conserved Lys-155 and Thr-156 residues in the phosphate-binding glycine-rich sequence of the F1-ATPase beta subunit of Escherichia coli

1 reference

12 December 2020

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.

1 reference

12 December 2020

β Subunit Glu-185 of Escherichia coli H+-ATPase (ATP Synthase) Is an Essential Residue for Cooperative Catalysis

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12 December 2020

Mode of inhibition of sodium azide on H+-ATPase of Escherichia coli

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12 December 2020

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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12 December 2020

Escherichia coli F1 ATPase is reversibly inhibited by intra- and intersubunit crosslinking: an approach to assess rotational catalysis.

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12 December 2020

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

1 reference

12 December 2020

Escherichia coli F0F1-ATPase. Residues involved in catalysis and coupling

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12 December 2020

Domains near ATP gamma phosphate in the catalytic site of H+-ATPase. Model proposed from mutagenesis and inhibitor studies.

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12 December 2020

Effect of dicyclohexylcarbodiimide on unisite and multisite catalytic activities of the adenosinetriphosphatase of Escherichia coli

1 reference

12 December 2020

F0F1-ATPase gamma subunit mutations perturb the coupling between catalysis and transport

1 reference

12 December 2020

The alpha/beta subunit interaction in H(+)-ATPase (ATP synthase). An Escherichia coli alpha subunit mutation (Arg-alpha 296-->Cys) restores coupling efficiency to the deleterious beta subunit mutant (Ser-beta 174-->Phe).

1 reference

12 December 2020

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

1 reference

12 December 2020

Inactivation of the bovine mitochondrial F1-ATPase with dicyclohexyl[14C]carbodiimide leads to the modification of a specific glutamic acid residue in the beta subunit

1 reference

12 December 2020

The mechanism of ATP synthase: a reassessment of the functions of the b and a subunits

1 reference

12 December 2020

Asymmetry of Escherichia coli F1-ATPase as a Function of the Interaction of α-β Subunit Pairs with the γ and ∊ Subunits

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12 December 2020

The gamma subunit of the Escherichia coli ATP synthase. Mutations in the carboxyl-terminal region restore energy coupling to the amino-terminal mutant gamma Met-23-->Lys.

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12 December 2020

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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12 December 2020

The proton-translocating ATPase of Escherichia coli

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12 December 2020

Mutations in Ser174 and the glycine-rich sequence (Gly149, Gly150, and Thr156) in the beta subunit of Escherichia coli H(+)-ATPase

1 reference

12 December 2020

Catalytic site of F1-ATPase of Escherichia coli. Lys-155 and Lys-201 of the beta subunit are located near the gamma-phosphate group of ATP in the presence of Mg2+.

1 reference

12 December 2020

Determination of the 1-ethyl-3-[(3-dimethylamino)propyl]-carbodiimide- induced cross-link between the beta and epsilon subunits of Escherichia coli F1-ATPase

1 reference

12 December 2020

Structure and Mechanism of F0F1-Type ATP Synthases and ATPases

1 reference

12 December 2020

Mechanism of ATP hydrolysis by beef heart mitochondrial ATPase. Rate constants for elementary steps in catalysis at a single site

1 reference

12 December 2020

Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution

1 reference

12 December 2020

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

1 reference

12 December 2020

Identifiers

DOI

10.1007/BF02113982

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28 September 2017

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