Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1. (Q41252025)

28 September 2017

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title

Subunit rotation in F0F1-ATP synthases as a means of coupling proton transport through F0 to the binding changes in F1. (English)

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28 September 2017

R L Cross

1

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PubMed ID

8951086

28 September 2017

T M Duncan

series ordinal

2

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28 September 2017

1 October 1996

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Journal of Bioenergetics and Biomembranes

28 September 2017

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28 September 2017

28

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28 September 2017

5

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28 September 2017

403-408

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https://scigraph.springernature.com/pub.10.1007/bf02113981

28 September 2017

0 references

cites work

Probing interactions of the Escherichia coli F0F1 ATP synthase beta and gamma subunits with disulphide cross-links.

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The proton conducting F0-part of bacterial ATP synthases

21 January 2018

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ATP synthases. Structure, reaction center, mechanism, and regulation of one of nature's most unique machines

21 January 2018

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12 December 2020

H+-ATPase activity of Escherichia coli F1F0 is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the F0 complex.

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12 December 2020

The nucleotide sequence of the atp genes coding for the F0 subunits a, b, c and the F1 subunit δ of the membrane bound ATP synthase of Escherichia coli

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12 December 2020

Column centrifugation generates an intersubunit disulfide bridge in Escherichia coli F1-ATPase

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12 December 2020

Subunit interaction during catalysis: alternating site cooperativity in photophosphorylation shown by substrate modulation of [18O]ATP species formation

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12 December 2020

Nucleotide sequence of the genes for F0 components of the proton-translocating ATPase from : Prediction of the primary structure of F0 subunits

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12 December 2020

Mutations in three of the putative transmembrane helices of subunit a of the Escherichia coli F1F0-ATPase disrupt ATP-driven proton translocation.

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12 December 2020

The unusual enzymology of ATP synthase

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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

The rotation of the alpha subunit of F1 relative to minor subunits is not involved in ATP synthesis. Evidence given by using an anti-alpha subunit monoclonal antibody

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12 December 2020

Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopy

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12 December 2020

The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activity

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12 December 2020

Subunit interaction during catalysis. Alternating site cooperativity of mitochondrial adenosine triphosphatase

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12 December 2020

Impaired proton conductivity resulting from mutations in the a subunit of F1F0 ATPase in Escherichia coli.

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12 December 2020

A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit.

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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.

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12 December 2020

ATP hydrolysis by membrane-bound Escherichia coli F0F1 causes rotation of the gamma subunit relative to the beta subunits

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

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Stoichiometry of subunits in the H+-ATPase complex of Escherichia coli.

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12 December 2020

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

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12 December 2020

Rotational dynamics of chloroplast ATP synthase in phospholipid vesicles

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12 December 2020

An alternating site sequence for oxidative phosphorylation suggested by measurement of substrate binding patterns and exchange reaction inhibitions

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12 December 2020

A new concept for energy coupling in oxidative phosphorylation based on a molecular explanation of the oxygen exchange reactions

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12 December 2020

The atp operon: nucleotide sequence of the genes for the γ, β, and ε subunits of Escherichia coli ATP synthase

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12 December 2020

The proton-translocating ATPase of Escherichia coli

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12 December 2020

Adenine nucleotide binding sites on beef heart F1-ATPase. Asymmetry and subunit location

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12 December 2020

Probes of catalytic site cooperativity during catalysis by the chloroplast adenosine triphosphate and the adenosine triphosphate synthase

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A perspective of the binding change mechanism for ATP synthesis

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

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12 December 2020

Rotation of nucleotide sites is not required for the enzymatic activity of chloroplast coupling factor 1.

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12 December 2020

Identifiers

DOI

10.1007/BF02113981

1 reference

28 September 2017

1 reference

PubMed ID

8951086