Observations of rotation within the FoF1‐ATP synthase: deciding between rotation of the Fo c subunit ring and artifact

No abstract is available for this paper.

• Publication year

  2000

• Venue

  FEBS Letters

• Publication date

  2000-03-31

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/S0014-5793(00)01336-3PMID 10745076
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

• The gamma subunit in chloroplast F(1)-ATPase can rotate in a unidirectional and counter-clockwise manner.

  1999cited by this paper
• The gamma-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli.

  1999cited by this paper
• Energy transduction in the sodium F-ATPase of Propionigenium modestum.

  1999cited by this paper
• The γ subunit in chloroplast F1‐ATPase can rotate in a unidirectional and counter‐clockwise manner

  1999cited by this paper
• Molecular Rotary Motors

  1999cited by this paper
• The γ-subunit rotation and torque generation in F1-ATPase from wild-type or uncoupled mutant Escherichia coli

  1999cited by this paper
• Molecular architecture of the rotary motor in ATP synthase.

  1999cited by this paper
• Mechanical rotation of the c subunit oligomer in ATP synthase (F0F1): direct observation.

  1999cited by this paper
• Rotation of Escherichia coli F(1)-ATPase.

  1999cited by this paper
• F 1-ATPase Is a Highly Efficient Molecular Motor that Rotates with Discrete 120 8 Steps

  1998cited by this paper
• F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps.

  1998cited by this paper
• Direct observation of the rotation of epsilon subunit in F1-ATPase.

  1998cited by this paper
• Direct Observation of the Rotation of ε Subunit in F1-ATPase*

  1998cited by this paper
• Rotation of a gamma-epsilon subunit domain in the Escherichia coli F1F0-ATP synthase complex. The gamma-epsilon subunits are essentially randomly distributed relative to the alpha3beta3delta domain in the intact complex.

  1997cited by this paper
• Direct observation of the rotation of F1-ATPase

  1997cited by this paper
• The ATP synthase--a splendid molecular machine.

  1997cited by this paper
• ATP synthase: an electrochemical transducer with rotatory mechanics.

  1997cited by this paper
• Conformational Changes in the Escherichia coli ATP Synthase (ECF1F0) Monitored by Nucleotide-dependent Differences in the Reactivity of Cys-87 of the γ Subunit in the Mutant βGlu-381 → Ala*

  1996cited by this paper
• The Stalk Region of the Escherichia coli ATP Synthase

  1996cited by this paper
• Conformational changes in the Escherichia coli ATP synthase (ECF1F0) monitored by nucleotide-dependent differences in the reactivity of Cys-87 of the gamma subunit in the mutant betaGlu-381 --> Ala.

  1996cited by this paper
• Intersubunit rotation in active F-ATPase

  1996cited by this paper
• 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.

  1995cited by this paper
• The γ subunit in the Escherichia coli ATP synthase complex (ECF1F0) extends through the stalk and contacts the c subunits of the F0 part

  1995cited by this paper
• Rotation of subunits during catalysis by Escherichia coli F1-ATPase.

  1995cited by this paper
• Disulfide Bond Formation between the COOH-terminal Domain of the Subunits and the and Subunits of the Escherichia coli F-ATPase

  1995cited by this paper
• A mechanism of proton translocation by F1F0 ATP synthases suggested by double mutants of the a subunit.

  1994cited by this paper
• Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

  1994cited by this paper
• Further examination of seventeen mutations in Escherichia coli F1-ATPase beta-subunit.

  1992cited by this paper
• Mutation of alanine 24 to serine in subunit c of the Escherichia coli F1F0-ATP synthase reduces reactivity of aspartyl 61 with dicyclohexylcarbodiimide.

  1991cited by this paper
• Ligand-dependent structural variations in Escherichia coli F1 ATPase revealed by cryoelectron microscopy.

  1990cited by this paper
• Directed mutagenesis of the strongly conserved aspartate 242 in the beta-subunit of Escherichia coli proton-ATPase.

  1988cited by this paper
• Labeling of the ATP synthase of Escherichia coli from the head-group region of the lipid bilayer.

  1987cited by this paper
• Rapid and efficient site-specific mutagenesis without phenotypic selection.

  1987cited by this paper
• New proteins involved in cell regulation by Ca2+ and phospholipids

  1986cited by this paper
• Rapid and efficient site-specific mutagenesis without phenotypic selection.

  1985cited by this paper
• Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit.

  1984cited by this paper
• Hypothesis the mecanism of ATP synthase conformational change by rotation of the b-subunit

  1984cited by this paper
• Integration of F1 and the membrane sector of the proton-ATPase of Escherichia coli. Role of subunit "b" (uncF protein).

  1983cited by this paper
• Mechanism of Flagellar Motor Rotation in Bacteria

  1982cited by this paper
• On the Structure and Genetics of the Proteolipid Subunit of the ATP Synthase Complex

  1981cited by this paper
• Energy-transducing H+-ATPase of Escherichia coli. Purification, reconstitution, and subunit composition.

  1979cited by this paper
• Changes in inhibitor sensitivity of the mitochondrial ATPase activity after detergent solubilisation

  1975cited by this paper

• Regulation machineries of ATP synthase from phototroph

  2020cites this paper
• Control of rotation of the F1FO-ATP synthase nanomotor by an inhibitory α-helix from unfolded ε or intrinsically disordered ζ and IF1 proteins

  2018cites this paper
• Biolayer interferometry of lipid nanodisc‐reconstituted yeast vacuolar H+‐ATPase

  2017cites this paper
• Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states

  2016cites this paper
• The a subunit of the A1AO ATP synthase of Methanosarcina mazei Gö1 contains two conserved arginine residues that are crucial for ATP synthesis.

  2015cites this paper
• ATPase/synthase activity of Paracoccus denitrificans Fo·F1 as related to the respiratory control phenomenon.

  2014cites this paper
• Arrayed lipid bilayer chambers allow single-molecule analysis of membrane transporter activity

  2014cites this paper
• A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective

  2014cites this paper
• DCCD inhibition mechanism of F o F 1 Single-molecule analysis of F o F 1 -ATP synthase inhibited by N , N -dicyclohexylcarbodiimide

  2013cites this paper
• Proton cycles through membranes in bacteria: Relationship between proton passive and active fluxes and their dependence on some external physico-chemical factors under fermentation

  2013cites this paper
• Single-molecule Analysis of F0F1-ATP Synthase Inhibited by N,N-Dicyclohexylcarbodiimide*

  2013cites this paper
• The chemo-mechanical coupled model for F(1)F(0)-motor.

  2012cites this paper
• Energy Transduction by the Two Molecular Motors of the F1Fo ATP Synthase

  2012cites this paper
• Monitoring transient elastic energy storage within the rotary motors of single FoF1-ATP synthase by DCO-ALEX FRET

  2012cites this paper
• Stabilization of Fo/Vo/Ao by a radial electric field

  2011cites this paper
• Rotation and structure of FoF1-ATP synthase.

  2011cites this paper
• ATP synthase: investigating its in vivo rotation and testing the inhibitory effects of diarylquinolines

  2011cites this paper
• JB Review Rotation and structure of F o F 1 -ATP synthase

  2011cites this paper
• ADVANCES IN F0F1-ATP SYNTHASE BIOLOGICAL PROTEIN NANOMOTOR: FROM MECHANISMS AND STRATEGIES TO POTENTIAL APPLICATIONS

  2009cites this paper
• Permeable cell assay: a method for high-throughput measurement of cellular ATP synthetic activity.

  2009cites this paper
• Domain compliance and elastic power transmission in rotary FOF1-ATPase

  2008cites this paper
• Construction and disulfide crosslinking of chimeric b subunits in the peripheral stalk of F1FO ATP synthase from Escherichia coli

  2008cites this paper
• Quantum dots for single-pair fluorescence resonance energy transfer in membrane- integrated EFoF1.

  2008cites this paper
• Molecular characterisation of SGCE-associated myoclonus-dystonia and PINK1-associated Parkinson's disease

  2008cites this paper
• ATP Synthesis by Oxidative Phosphorylation

  2007cites this paper
• Proton Translocating ATPases

  2006cites this paper
• An Efficient Method for Quantitative Determination of Cellular ATP Synthetic Activity

  2006cites this paper
• Coupling Proton Movement to ATP Synthesis in the Chloroplast ATP Synthase

  2005cites this paper
• Proton slip in the ATP synthase of Rhodobacter capsulatus: induction, proton conduction, and nucleotide dependence.

  2005cites this paper
• The proton-driven rotor of ATP synthase: ohmic conductance (10 fS), and absence of voltage gating.

  2004cites this paper
• Fluorescent probes applied to catalytic cooperativity in ATP synthase.

  2004cites this paper
• Rotation of F1-ATPase: how an ATP-driven molecular machine may work.

  2004cites this paper
• Close Proximity of a Cytoplasmic Loop of Subunit awith c Subunits of the ATP Synthase fromEscherichia coli *

  2003cites this paper
• Single Molecule Spectroscopy

  2003cites this paper
• Conformational change of the chloroplast ATP synthase on the enzyme activation process detected by the trypsin sensitivity of the gamma subunit.

  2003cites this paper
• Electrostatic interactions in catalytic centers of F1-ATPase

  2003cites this paper
• The ATP synthase: Parts and properties of a rotary motor

  2003cites this paper
• ATP synthesis driven by proton transport in F1F0‐ATP synthase

  2003cites this paper
• Rotation of the Proteolipid Ring in the V-ATPase*

  2003cites this paper
• The H+-ATPase from chloroplasts: effect of different reconstitution procedures on ATP synthesis activity and on phosphate dependence of ATP synthesis.

  2002cites this paper
• NMR investigations of subunit c of the ATP synthase from Propionigenium modestum in chloroform/methanol/water (4 : 4 : 1).

  2002cites this paper
• F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring.

  2002cites this paper
• Rotation of the c Subunit Oligomer in EF0EF1 Mutant cD61N*

  2002cites this paper
• Mechanism of the F(1)F(0)-type ATP synthase, a biological rotary motor.

  2002cites this paper
• Coupled rotation within single F0F1 enzyme complexes during ATP synthesis or hydrolysis

  2002cites this paper
• Genetic fusions of globular proteins to the epsilon subunit of the Escherichia coli ATP synthase: Implications for in vivo rotational catalysis and epsilon subunit function.

  2002cites this paper
• The Na(+)-translocating F(1)F(0) ATP synthase of Propionigenium modestum: mechanochemical insights into the F(0) motor that drives ATP synthesis.

  2001cites this paper
• The rotor in the membrane of the ATP synthase and relatives

  2001cites this paper
• ATP synthase — a marvellous rotary engine of the cell

  2001cites this paper
• The central plug in the reconstituted undecameric c cylinder of a bacterial ATP synthase consists of phospholipids

  2001cites this paper
• Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: angular torque profile of the enzyme.

  2001cites this paper
• Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the FO sector of Escherichia coli ATP synthase

  2001cites this paper
• Rotation of a complex of the gamma subunit and c ring of Escherichia coli ATP synthase. The rotor and stator are interchangeable.

  2001cites this paper
• Large conformational changes of the ɛ subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

  2001cites this paper
• Role of the ATP synthase alpha-subunit in conferring sensitivity to tentoxin.

  2001cites this paper
• Rotation of the c subunit oligomer in fully functional F1Fo ATP synthase.

  2001cites this paper
• Assembled F1-(alpha beta ) and Hybrid F1-alpha 3beta 3gamma -ATPases from Rhodospirillum rubrum alpha, wild type or mutant beta, and chloroplast gamma subunits. Demonstration of Mg2+versus Ca2+-induced differences in catalytic site structure and function.

  2001cites this paper
• The Rotary Machine in the Cell, ATP Synthase* 210

  2001cites this paper
• Formation and properties of hybrid photosynthetic F1-ATPases. Demonstration of different structural requirements for stimulation and inhibition by tentoxin.

  2001cites this paper
• Viscoelastic dynamics of actin filaments coupled to rotary F-ATPase: curvature as an indicator of the torque.

  2001cites this paper
• Inter‐subunit rotation and elastic power transmission in F0F1‐ATPase

  2001cites this paper
• Osmomechanics of the Propionigenium modestum Fo Motor

  2000cites this paper
• Mutational Analysis of Subunit G (Vma10p) of the Yeast Vacuolar H+-ATPase*

  2000cites this paper
• F1F0-ATP Synthase—Stalking Mind and Imagination

  2000cites this paper
• ATP synthase. Is revolution effective?

  2000cites this paper
• Structural Changes during ATP Hydrolysis Activity of the ATP Synthase fromEscherichia colias Revealed by Fluorescent Probes

  2000cites this paper
• Critical evaluation of the one- versus the two-channel model for the operation of the ATP synthase's F(o) motor.

  2000cites this paper
• The Activity of the ATP Synthase from Escherichia coli Is Regulated by the Transmembrane Proton Motive Force*

  2000cites this paper
• The alpha/beta interfaces of alpha(1)beta(1), alpha(3)beta(3), and F1: domain motions and elastic energy stored during gamma rotation.

  2000cites this paper
• Insights into the Rotary Catalytic Mechanism of F0F1 ATP Synthase from the Cross-linking of Subunits b and c in the Escherichia coli Enzyme*

  2000cites this paper
• Movement of the Helical Domain of the ε Subunit Is Required for the Activation of Thermophilic F1-ATPase*

  2000cites this paper
• F1 and F0 connections in the bovine mitochondrial ATP synthase: the role of the of alpha subunit N-terminus, oligomycin-sensitivity conferring protein (OCSP) and subunit d.

  2000cites this paper
• The Catalytic Transition State in ATP Synthase

  2000cites this paper
• Molecular Characterization of the Yeast Vacuolar H+-ATPase Proton Pore*

  2000cites this paper
• A Biological Molecular Motor, Proton-Translocating ATP Synthase: Multidisciplinary Approach for a Unique Membrane Enzyme

  2000cites this paper
• Movement of the helical domain of the epsilon subunit is required for the activation of thermophilic F1-ATPase.

  2000cites this paper
• ATP synthase

  2000cites this paper
• The rotary mechanism of ATP synthase.

  2000cites this paper
• ATP synthase: what dictates the size of a ring?

  2000cites this paper
• The Structural and Functional Connection between the Catalytic and Proton Translocating Sectors of the Mitochondrial F1F0-ATP Synthase

  2000cites this paper