Glutamate residues at positions 219 and 252 in the a-subunit of the Escherichia coli ATP synthase are not functionally equivalent

scientific article published on March 1998

Glutamate residues at positions 219 and 252 in the a-subunit of the Escherichia coli ATP synthase are not functionally equivalent is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1016/S0005-2728(97)00101-1
P698PubMed publication ID9518621

P2093author name stringG B Cox
S M Howitt
L P Hatch
P2860cites workThe UNC operon nucleotide sequence, regulation and structure of ATP-synthaseQ40111464
Oxidative phosphorylation by mutant Escherichia coli membranes with impaired proton permeabilityQ42037664
The function of ubiquinone in Escherichia coliQ42172262
The transmembrane topology of the a [corrected] subunit from the ATPase in Escherichia coli analyzed by PhoA protein fusionsQ44849296
The proton pore of the F0F1-ATPase of Escherichia coli: Ser-206 is not required for proton translocation.Q54740051
Role of the carboxyl terminal region of H+-ATPase (F0F1a subunit from Escherichia coliQ67897409
Mutational analysis of the function of the a-subunit of the F0F1-APPase of Escherichia coliQ68409126
DNA sequencing with chain-terminating inhibitorsQ22066207
A rapid alkaline extraction procedure for screening recombinant plasmid DNAQ24614998
2 New M13 vectors for cloningQ27861042
Hybridization between Escherichia coli and Shigella.Q33972142
An acidic or basic amino acid at position 26 of the b subunit of Escherichia coli F1F0-ATPase impairs membrane proton permeability: suppression of the uncF469 nonsense mutationQ36287927
Second-site revertants of an arginine-210 to lysine mutation in the a subunit of the F0F1-ATPase from Escherichia coli: implications for structureQ37254308
The proton-translocating ATPase of Escherichia coliQ37855044
The coupling of the relative movement of the a and c subunits of the F0 to the conformational changes in the F1-ATPaseQ38465000
The essential arginine residue at position 210 in the alpha subunit of the Escherichia coli ATP synthase can be transferred to position 252 with partial retention of activityQ38466250
The role of arginine in the conserved polar loop of the c-subunit of the Escherichia coli H(+)-ATPaseQ38469790
The proton pore in the Escherichia coli F0F1-ATPase: a requirement for arginine at position 210 of the a-subunitQ38475847
The mechanism of ATP synthase: a reassessment of the functions of the b and a subunitsQ38477714
Partial diploids of Escherichia coli carrying normal and mutant alleles affecting oxidative phosphorylationQ39817358
A mutation affecting a second component of the F0 portion of the magnesium ion-stimulated adenosine triphosphatase of Escherichia coli K12. The uncC424 alleleQ39820637
P433issue3
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)217-223
P577publication date1998-03-01
P1433published inBiochimica et Biophysica ActaQ864239
P1476titleGlutamate residues at positions 219 and 252 in the a-subunit of the Escherichia coli ATP synthase are not functionally equivalent
P478volume1363

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cites work (P2860)
Q33933707A model for the structure of subunit a of the Escherichia coli ATP synthase and its role in proton translocation.
Q37312462A more robust version of the Arginine 210-switched mutant in subunit a of the Escherichia coli ATP synthase.
Q43959096A point mutation in the ATP synthase of Rhodobacter capsulatus results in differential contributions of Delta(pH) and Delta(phi) in driving the ATP synthesis reaction
Q50467127Expanding the clinical phenotypes of MT-ATP6 mutations.
Q34478495Mutagenic analysis of the F0 stator subunits
Q44588220The role of transmembrane span 2 in the structure and function of subunit a of the ATP synthase from Escherichia coli.

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