Energy-dependent transformation of F0.F1-ATPase in Paracoccus denitrificans plasma membranes (Q44727114)

5 December 2017

Energy-dependent transformation of F0.F1-ATPase in Paracoccus denitrificans plasma membranes (English)

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5 December 2017

Paracoccus denitrificans

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author name string

Tatyana V Zharova

series ordinal

1

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PubMed ID

14722115

5 December 2017

Andrei D Vinogradov

series ordinal

2

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PubMed ID

14722115

5 December 2017

language of work or name

English

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publication date

13 January 2004

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Journal of Biological Chemistry

5 December 2017

6

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based on heuristic

inferred from page(s)

published in

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5 December 2017

279

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5 December 2017

13

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5 December 2017

12319-12324

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ATP synthases in the year 2000: evolving views about the structures of these remarkable enzyme complexes

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The structure of the H(+)-ATP synthase from chloroplasts and its subcomplexes as revealed by electron microscopy

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F(0)F(1)-ATP synthase: general structural features of 'ATP-engine' and a problem on free energy transduction

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An inhibitory high affinity binding site for ADP in the oligomycin-sensitive ATPase of beef heart submitochondrial particles

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Kinetic mechanism of mitochondrial adenosine triphosphatase. ADP-specific inhibition as revealed by the steady-state kinetics

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

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Interaction of Mg2+ with F0.F1 mitochondrial ATPase as related to its slow active/inactive transition

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The ADP that binds tightly to nucleotide-depleted mitochondrial F1-ATPase and inhibits catalysis is bound at a catalytic site

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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

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Adenine nucleotide-binding sites on mitochondrial F1-ATPase: studies of the inactive complex formed upon binding ADP at a catalytic site

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Analysis of time-dependent change of Escherichia coli Fl-ATPase activity and its relationship with apparent negative cooperativity

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Pre-steady state kinetics of nucleotide-triphosphate hydrolysis by mitochondrial F1-ATPase from yeast

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

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Inhibition of steady-state mitochondrial ATP synthesis by bicarbonate, an activating anion of ATP hydrolysis

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Thermophilic F1-ATPase is activated without dissociation of an endogenous inhibitor, epsilon subunit.

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F0F1-ATPase/synthase is geared to the synthesis mode by conformational rearrangement of epsilon subunit in response to proton motive force and ADP/ATP balance

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Isolated epsilon subunit of thermophilic F1-ATPase binds ATP.

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The inhibitor-sensitivity of the plasma-membrane adenosine triphosphatase of Paracoccus denitrificans: comparison with the mitochondrial adenosine triphosphatase [proceedings]

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Tightly bound nucleotides of the energy-transducing ATPase, and their role in oxidative phosphorylation. I. The Paracoccus denitrificans system

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Kinetics of oxidative phosphorylation in Paracoccus denitrificans. 1. Mechanism of ATP synthesis at the active site(s) of F0F1-ATPase

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Kinetics of oxidative phosphorylation in Paracoccus denitrificans. 2. Evidence for a kinetic and thermodynamic modulation of F0F1-ATPase by the activity of the respiratory chain.

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ATP synthesis by F0F1-ATP synthase independent of noncatalytic nucleotide binding sites and insensitive to azide inhibition

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Proton-translocating ATP-synthase of Paracoccus denitrificans: ATP-hydrolytic activity

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The use of cyanine dyes for the determination of membrane potentials in cells, organelles, and vesicles

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58 Uncouplers of oxidative phosphorylation

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Does the gamma subunit move to an abortive position of ATP hydrolysis when the F1.ADP.Mg complex isomerizes to the inactive F1*.ADP.Mg complex?

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Catalytic site forms and controls in ATP synthase catalysis

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The noncatalytic site-deficient alpha3beta3gamma subcomplex and FoF1-ATP synthase can continuously catalyse ATP hydrolysis when Pi is present

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The presence of phosphate at a catalytic site suppresses the formation of the MgADP-inhibited form of F(1)-ATPase

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Large conformational changes of the epsilon subunit in the bacterial F1F0 ATP synthase provide a ratchet action to regulate this rotary motor enzyme

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The ATPase as an irreversible component in electron transport linked ATP synthesis

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Properties of bound inorganic phosphate on bovine mitochondrial F1F0-ATP synthase

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Control of mitochondrial ATP synthesis in the heart

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Deletion of mitochondrial ATPase inhibitor in the yeast Saccharomyces cerevisiae decreased cellular and mitochondrial ATP levels under non-nutritional conditions and induced a respiration-deficient cell-type

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Three adenine nucleotide binding sites in F1-F0 mitochondrial ATPase as revealed by presteady-state and steady-state kinetics of ATP hydrolysis. Evidence for two inhibitory ADP-specific noncatalytic sites

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ATP synthesis catalyzed by the mitochondrial F1-F0 ATP synthase is not a reversal of its ATPase activity

21 January 2018

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The epsilon subunit of the F(1)F(0) complex of Escherichia coli. cross-linking studies show the same structure in situ as when isolated

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Sulfite and membrane energization induce two different active states of the Paracoccus denitrificans F0F1-ATPase

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Sulfite stimulates the ATP hydrolysis activity of but not proton translocation by the ATP synthase of Rhodobacter capsulatus and interferes with its activation by delta muH+

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The effect of sulfite on the ATP hydrolysis and synthesis activities in chloroplasts and cyanobacterial membrane vesicles can be explained by competition with phosphate

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Energy-dependent transformation of the catalytic activities of the mitochondrial F0 x F1-ATP synthase

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Oxidative phosphorylation coupled to oxygen uptake and nitrate reduction in Micrococcus denitrificans

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Respiratory control in membrane particles from Micrococcus denitrificans

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Identifiers

DOI

10.1074/JBC.M311397200

1 reference

5 December 2017

1 reference

PubMed ID

14722115