(Q34144700)

31 July 2017

A research journey with ATP synthase (English)

1 reference

31 July 2017

Paul D Boyer

1

1 reference

PubMed ID

12181328

31 July 2017

language of work or name

English

0 references

publication date

13 August 2002

1 reference

Journal of Biological Chemistry

31 July 2017

1 reference

31 July 2017

277

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31 July 2017

42

1 reference

31 July 2017

39045-39061

1 reference

Structure of the bis(Mg2+)-ATP-oxalate complex of the rabbit muscle pyruvate kinase at 2.1 A resolution: ATP binding over a barrel

31 July 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Mitochondrial oxidations and energy coupling

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Oxidative phosphorylation in mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Electron transport phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

The rapid labeling of adenosine triphosphate by 32P-labeled inorganic phosphate and the exchange of phosphate oxygens as related to conformational coupling in oxidative phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

The characterization of myosin-product complexes and of product-release steps during the magnesium ion-dependent adenosine triphosphatase reaction

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Oxygen exchange in the gamma-phosphoryl group of protein-bound ATP during Mg2+-dependent adenosine triphosphatase activity of myosin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

A chemiosmotic molecular mechanism for proton-translocating adenosine triphosphatases.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Energy transduction and proton translocation by adenosine triphosphatases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Proton translocation mechanisms and energy transduction by adenosine triphosphatases: An answer to criticisms

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

A model for conformational coupling of membrane potential and proton translocation to ATP synthesis and to active transport

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Occurrence of an uncoupler-resistant intermediate type of phosphate-water oxygen exchange reaction catalyzed by heart submitochondrial particles

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Medium ADP and not ADP already tightly bound to phylakoid membranes forms the initial ATP in chloroplast phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Demonstration of a transitory tight binding of ATP and of committed P(i) and ADP during ATP synthesis by chloroplasts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

F1 ATPase from the thermophilic bacterium PS3 (TF1) shows ATP modulation of oxygen exchange

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Vacuolar ATPases, like F1,F0-ATPases, show a strong dependence of the reaction velocity on the binding of more than one ATP per enzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Bound adenosine 5'-triphosphate formation, bound adenosine 5'-diphosphate and inorganic phosphate retention, and inorganic phosphate oxygen exchange by chloroplast adenosinetriphosphatase in the presence of Ca2+ or Mg2+.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Active/inactive state transitions of mitochondrial ATPase molecules influenced by Mg2+ , anions and aurovertin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Interaction of Mg+2 with beef heart mitochondrial ATPase (F1)

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Kinetic mechanism of mitochondrial adenosine triphosphatase. Inhibition by azide and activation by sulphite

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

The mechanism of stimulation of MgATPase activity of chloroplast F1-ATPase by non-catalytic adenine-nucleotide binding. Acceleration of the ATP-dependent release of inhibitory ADP from a catalytic site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Adenine nucleotide binding sites on beef heart F1 ATPase: photoaffinity labeling of beta-subunit Tyr-368 at a noncatalytic site and beta Tyr-345 at a catalytic site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Catalytic and noncatalytic nucleotide binding sites of chloroplast F1 ATPase. Photoaffinity labeling and peptide sequencing

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Catalytic and noncatalytic nucleotide binding sites of the Escherichia coli F1 ATPase. Amino acid sequences of beta-subunit tryptic peptides labeled with 2-azido-ATP.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Tightly bound 2-azido-adenine nucleotides at catalytic and noncatalytic sites of the rat liver F1 ATPase label adjacent tryptic peptides of the beta subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Chloroplast F1 ATPase has more than three nucleotide binding sites, and 2-azido-ADP or 2-azido-ATP at both catalytic and noncatalytic sites labels the beta subunit

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

The alpha 3(beta Y341W)3 gamma subcomplex of the F1-ATPase from the thermophilic Bacillus PS3 fails to dissociate ADP when MgATP is hydrolyzed at a single catalytic site and attains maximal velocity when three catalytic sites are saturated with MgAT

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Catalytic site occupancy during ATP synthase catalysis

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

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.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Direct observation of the rotation of F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Functional and idling rotatory motion within F1-ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

The ATP synthase--a splendid molecular machine

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Crystallization of F1-ATPase from Bovine Heart Mitochondria

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

Reversal and Mechanism of Oxidative Phosphorylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.X200001200

21 January 2018

Identifiers

DOI

10.1074/JBC.X200001200

1 reference

31 July 2017

1 reference

PubMed ID

12181328