pH dependence of H+ conduction through the membrane moiety of the H+-ATPase (F0 . F1) and effects of tyrosyl residue modification

scientific article published in March 1981

pH dependence of H+ conduction through the membrane moiety of the H+-ATPase (F0 . F1) and effects of tyrosyl residue modification is …
instance of (P31):
scholarly articleQ13442814

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P698PubMed publication ID6451621

P2093author name stringHamamoto T
Sone N
Kagawa Y
P433issue6
P407language of work or nameEnglishQ1860
P304page(s)2873-2877
P577publication date1981-03-01
P1433published inJournal of Biological ChemistryQ867727
P1476titlepH dependence of H+ conduction through the membrane moiety of the H+-ATPase (F0 . F1) and effects of tyrosyl residue modification
P478volume256

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cites work (P2860)
Q41382721All three subunits are required for the reconstitution of an active proton channel (F0) of Escherichia coli ATP synthase (F1F0).
Q39466352Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits
Q34187841Determination of proton flux and conductance at pH 6.8 through single FO sectors from Escherichia coli
Q70566152Effect of chemical modifiers of amino acid residues on proton conduction by the H+-ATPase of mitochondria
Q40103772Energy coupling to ATP synthesis by the proton-translocating ATPase
Q40103755Molecular mechanism of proton translocation by the cytochrome system and the ATPase of mitochondria. Role of proteins
Q81575834Protons, proteins and ATP
Q40107164The proton-ATPase of bacteria and mitochondria
Q40286222The proton-driven rotor of ATP synthase: ohmic conductance (10 fS), and absence of voltage gating

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