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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Effects of carbon source on expression of F0 genes and on the stoichiometry of the c subunit in the F1F0 ATPase of Escherichia coli The vacuolar H+-ATPase: a universal proton pump of eukaryotes Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase The rotary mechanism of the ATP synthase.Filming biomolecular processes by high-speed atomic force microscopy Structure of the membrane domain of subunit b of the Escherichia coli F0F1 ATP synthase The structure of the chloroplast F1-ATPase at 3.2 A resolution The structure and nucleotide occupancy of bovine mitochondrial F(1)-ATPase are not influenced by crystallisation at high concentrations of nucleotide Structure of Ala(20) --> Pro/Pro(64) --> Ala substituted subunit c of Escherichia coli ATP synthase in which the essential proline is switched between transmembrane helices Structures of the thermophilic F1-ATPase subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1 Structure of the c14 Rotor Ring of the Proton Translocating Chloroplast ATP Synthase The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis Yeast cells depleted in Atp14p fail to assemble Atp6p within the ATP synthase and exhibit altered mitochondrial cristae morphology.Proton translocation driven by ATP hydrolysis in V-ATPases Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review)Molecular motors: turning the ATP motor Cysteine-mediated cross-linking indicates that subunit C of the V-ATPase is in close proximity to subunits E and G of the V1 domain and subunit a of the V0 domain Regulation of the F0F1-ATP synthase: the conformation of subunit epsilon might be determined by directionality of subunit gamma rotation Intragenic and intergenic suppression of the Escherichia coli ATP synthase subunit a mutation of Gly-213 to Asn: functional interactions between residues in the proton transport site Purine but not pyrimidine nucleotides support rotation of F(1)-ATPase.F1-ATPase of Escherichia coli: the ε- inhibited state forms after ATP hydrolysis, is distinct from the ADP-inhibited state, and responds dynamically to catalytic site ligands.A rotor-stator cross-link in the F1-ATPase blocks the rate-limiting step of rotational catalysis Intergenic suppression of the gammaM23K uncoupling mutation in F0F1 ATP synthase by betaGlu-381 substitutions: the role of the beta380DELSEED386 segment in energy coupling.Folding-based molecular simulations reveal mechanisms of the rotary motor F1-ATPase.The regulator of the F1 motor: inhibition of rotation of cyanobacterial F1-ATPase by the epsilon subunit.Temperature-sensitive reaction intermediate of F1-ATPase.Single-molecule study on the temperature-sensitive reaction of F1-ATPase with a hybrid F1 carrying a single beta(E190D).The gamma subunit in chloroplast F(1)-ATPase can rotate in a unidirectional and counter-clockwise manner.Microsecond time scale rotation measurements of single F1-ATPase molecules NMR investigations of subunit c of the ATP synthase from Propionigenium modestum in chloroform/methanol/water (4 : 4 : 1).Direct observation of the rotation of epsilon subunit in F1-ATPase.Improving FRET-based monitoring of single chemomechanical rotary motors at work.F1F0-ATP synthases of alkaliphilic bacteria: lessons from their adaptations.Activation of pausing F1 motor by external force Resolution of distinct rotational substeps by submillisecond kinetic analysis of F1-ATPase.Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation.Rapid hydrolysis of ATP by mitochondrial F1-ATPase correlates with the filling of the second of three catalytic sites A research journey with ATP synthase.Subunit rotation of ATP synthase embedded in membranes: a or beta subunit rotation relative to the c subunit ring.Rotation and structure of FoF1-ATP synthase.

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P2860

Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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1995 nî lūn-bûn

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1995 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

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1995年の論文

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1995年論文

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1995年論文

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1995年論文

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1995年論文

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1995年论文

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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Proceedings of the National Academy of Sciences of the United States of America

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Rotation of subunits during catalysis by Escherichia coli F1-ATPase

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M L Hutcheon

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R L Cross

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T M Duncan

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V V Bulygin

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Y Zhou

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P2860

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

Cleavage of structural proteins during the assembly of the head of bacteriophage T4

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

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

A simplification of the protein assay method of Lowry et al. which is more generally applicable

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

Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble dinitrophenol-stimulated adenosine triphosphatase.

The proton-translocating ATPase of Escherichia coli.

A perspective of the binding change mechanism for ATP synthesis.

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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7479919

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Escherichia coli

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40551

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