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Literature summary for 7.1.2.2 extracted from

  • Kim, Y.; Konno, H.; Sugano, Y.; Hisabori, T.
    Redox regulation of rotation of the cyanobacterial F1-ATPase containing thiol regulation switch (2011), J. Biol. Chem., 286, 9071-9078.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 7.1.2.2

Activating Compound

Activating Compound Comment Organism Structure
lauryl dimethylamine-N-oxide
-
 Thermosynechococcus vestitus
additional information by reduction, both the alpha3beta3gammaredox complex and the purified CF1 show a 2.7fold activation Thermosynechococcus vestitus

Cloned(Commentary)

Cloned (Comment) Organism
expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex Spinacia oleracea
expression of recombinant His-tagged chimeric alpha3beta3gammaredox complex Thermosynechococcus vestitus

Protein Variants

Protein Variants Comment Organism
additional information construction of a chimeric F1 complex using cyanobacterial F1 from Thermosynechoccus elongatus, which mimics the regulatory properties of the chloroplast F1-ATPase introducing the regulatory element of spinach F1-ATPase gamma subunit, residues 187-210. The redox state of the gamma-subunit does not affect the ATP-binding rate to the catalytic site(s) and the torque for rotation. The long pauses caused by ADP inhibition are frequently observed in the oxidized state. The duration of continuous rotation is relatively shorter in the oxidized recombinant alpha3beta3gammaredox complex. The chimeric complex becomes biotinylated and shows higher stability for purification and assay experiments than the cyanobacterial wild-type, overview Spinacia oleracea
additional information construction of a chimeric F1 complex using the cyanobacterial F1, which mimics the regulatory properties of the chloroplast F1-ATPase from Spinacia oleracea introducing the regulatory element of the higher plant F1-ATPase gamma subunit, residues187-210. The redox state of the gamma-subunit does not affect the ATP-binding rate to the catalytic site(s) and the torque for rotation. The long pauses caused by ADP inhibition are frequently observed in the oxidized state. The duration of continuous rotation is relatively shorter in the oxidized recombinant alpha3beta3gammaredox complex. The chimeric complex becomes biotinylated and shows higher stability for purification and assay experiments than the cyanobacterial wild-type, overview Thermosynechococcus vestitus

Inhibitors

Inhibitors Comment Organism Structure
ADP
-
 Spinacia oleracea
ADP inhibition of the enzyme causing pauses in the ATP synthesis or hydrolysis, reversible by lauryl dimethylamine-N-oxide Thermosynechococcus vestitus

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Spinacia oleracea 9507
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Spinacia oleracea
Mg2+ required Thermosynechococcus vestitus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + H+/in Thermosynechococcus vestitus
-
 ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in Spinacia oleracea F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis ADP + phosphate + H+/out
-
 r

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-
Thermosynechococcus vestitus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged chimeric alpha3beta3gammaredox complex by nickel affinity chromatography and gel filtration Spinacia oleracea
recombinant His-tagged chimeric alpha3beta3gammaredox complex by nickel affinity chromatography and gel filtration Thermosynechococcus vestitus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + H+/in
-
 Spinacia oleracea ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in
-
 Thermosynechococcus vestitus ADP + phosphate + H+/out
-
 r
ATP + H2O + H+/in F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis Spinacia oleracea ADP + phosphate + H+/out
-
 r

Synonyms

Synonyms Comment Organism
F1-ATP synthase
-
 Spinacia oleracea
F1-ATP synthase
-
 Thermosynechococcus vestitus
F1-ATPase
-
 Spinacia oleracea
F1-ATPase
-
 Thermosynechococcus vestitus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 ATP hydrolysis assay at Spinacia oleracea
25
-
 ATP hydrolysis assay at Thermosynechococcus vestitus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
 ATP hydrolysis assay at Spinacia oleracea
7.5
-
 ATP hydrolysis assay at Thermosynechococcus vestitus

General Information

General Information Comment Organism
metabolism F1-ATPase is equipped with a special mechanism that prevents the wasteful reverse reaction, ATP hydrolysis, when there is insufficient proton motive force to drive ATP synthesis. Chloroplast F1-ATPase is subject to redox regulation, whereby ATP hydrolysis activity is regulated by formation and reduction of the disulfide bond located on the gamma-subunit, molecular mechanism, overview Spinacia oleracea