Quantitative evaluation of the intrinsic uncoupling modulated by ADP and Pi in the reconstituted ATP synthase of Escherichia coli

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1807, Issue 1, 2011, Pages 130-143

  D'Alessandro, Manuela ^a,b   Turina, Paola ^a   Melandri, B Andrea ^a  

^a UNIVERSITY OF BOLOGNA   (Italy)

^b INSTITUT DE GÉNÉTIQUE ET DE BIOLOGIE MOLÉCULAIRE ET CELLULAIRE   (France)

Author keywords

ATP synthase; Coupling ratio; E. coli; H+ ATP; Intrinsic uncoupling; Proteoliposomes

Indexed keywords

ADENOSINE DIPHOSPHATE; PROTON PUMP; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; PYRUVATE KINASE;

ACIDIFICATION; ARTICLE; BINDING AFFINITY; COUPLING FACTOR; ENZYME ACTIVITY; ESCHERICHIA COLI; NONHUMAN; NUCLEIC ACID BASE SUBSTITUTION; PH; PRIORITY JOURNAL; PROTEIN HYDROLYSIS; PROTEOLIPOSOME; PROTON TRANSPORT; QUANTITATIVE ANALYSIS;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CATALYSIS; CELL MEMBRANE; CHLOROPLASTS; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; HYDROLYSIS; KINETICS; PHOSPHATES; PHOSPHORYLATION; PLASMIDS; PROTON-TRANSLOCATING ATPASES; PYRUVATE KINASE;

ESCHERICHIA COLI;

EID: 78249277866     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.08.011     Document Type: Article

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