Literature summary for 7.1.2.2 extracted from

Mitome, N.; Ono, S.; Sato, H.; Suzuki, T.; Sone, N.; Yoshida, M.
Essential arginine residue of the Fo-a subunit in FoF1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the Fo proton channel (2010), Biochem. J., 430, 171-177.

Search for more literature for 7.1.2.2

Cloned(Commentary)

Cloned (Comment)	Organism
expression of FoF1, tagged with His10 at the beta-subunit N-terminus, in Escherichia coli strain DK8	Bacillus sp. PS3

Protein Variants

Protein Variants	Comment	Organism
alphaR169A	thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation. (c10-alphaR169E)FoF1 is always more efficient in proton translocation than (c10-alphaR169A)FoF1	Bacillus sp. PS3
alphaR169E	thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation. (c10-alphaR169E)FoF1 is always more efficient in proton translocation than (c10-alphaR169A)FoF1	Bacillus sp. PS3
alphaR169G/Q217R	substitutions in the gamma subunit of Fo, the mutation blocks the passive proton translocation	Bacillus sp. PS3
alphaR169X	thermophilic FoF1s with substitution of this arginine 169 in Fo alpha subunit with other residues cannot catalyse proton-coupled reactions. Mutants with substitution of this arginine residue by a small, e.g. glycine, alanine, valine, or acidic, e.g. glutamate, residue mediate the passive proton translocation	Bacillus sp. PS3
gammaE56Q	substitution of Glu56 in the gamma subunit of Fo, the mutation blocks the passive proton translocation	Bacillus sp. PS3

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	-	Bacillus sp. PS3	16020	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Bacillus sp. PS3

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ADP + phosphate + H+/out	Bacillus sp. PS3	-	ATP + H2O + H+/in	-	r

Organism

Organism	UniProt	Comment	Textmining
Bacillus sp. PS3	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
recombinant His10-tagged FoF1, from Echerichia coli strain DK8 by nickel affinity chromatography	Bacillus sp. PS3

Renatured (Commentary)

Renatured (Comment)	Organism
stripping of F1 and Fo from recombinant membrane fragments, and functional purified FoF1s reconstitutions in proteoliposomes, suspended in 10 mM HEPES/NaOH, pH 7.5, 0.25 M sucrose, and 5 mM MgSO4, at 25°C	Bacillus sp. PS3

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ADP + phosphate + H+/out	-	Bacillus sp. PS3	ATP + H2O + H+/in	-	r
additional information	an essential arginine residue R169 of the Fo-alpha subunit in FoF1-ATP synthase has a role to prevent the proton shortcut without c-ring rotation in the Fo proton channel, overview	Bacillus sp. PS3	?	-	?

Synonyms

Synonyms	Comment	Organism
FoF1	-	Bacillus sp. PS3
FoF1-ATP synthase	-	Bacillus sp. PS3

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
45	-	ATPase assay at	Bacillus sp. PS3

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	ATPase assay at	Bacillus sp. PS3

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Release 2023.1 (January 2023)