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October 1, 1981Journal of Biological ChemistryOpen Access

The defective proton-ATPase of uncA mutants of Escherichia coli. Studies of nucleotide binding sites, bound aurovertin fluorescence, and labeling of essential residues of the purified F1-ATPase.

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Authors

JWJohn G. WiseSouthern Methodist UniversityLLLisa R. LatchneyUniversity of Rochester Medical CenterASA.E. SeniorAmerican University of Antigua

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Wise et al. (1981) studied this question.

synapsesocial.com/papers/6a6ff66235aa2c282ce1459fhttps://doi.org/10.1016/s0021-9258(19)68630-8
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Also Consider

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  1. 1Reconstitution of a functional coupling factor from the isolated subunits of Escherichia coli F1 ATPase.1980 · 275 citations
  2. 2The <i>uncA</i> gene codes for the α-subunit of the adenosine triphosphatase of <i>Escherichia coli</i>. Electrophoretic analysis of <i>uncA</i> mutant strains1979 · 76 citations
  3. 3The Mitochondrial ATPase1975 · 215 citations
  4. 4Interaction of Escherichia coli adenosine triphosphatase with aurovertin and citreoviridin: inhibition and fluorescence studies1980 · 40 citations
  5. 5The ATP Synthetase of Escherichia coli K12: Purification of the Enzyme and Reconstitution of Energy-Transducing Activities1979 · 97 citations