Energy coupling, turnover, and stability of the F0F1 ATP synthase are dependent on the energy of interaction between γ and β subunits

Journal of Biological Chemistry

Volumn 272, Issue 4, 1997, Pages 2300-2306

  Al Shawi, Marwan K ^a   Ketchum, Christian J ^a   Nakamoto, Robert K ^a  

^a UNIVERSITY OF VIRGINIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; MUTANT PROTEIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME ASSAY; ESCHERICHIA COLI; GENE MUTATION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; THERMODYNAMICS; X RAY CRYSTALLOGRAPHY;

HYDROLYSIS; KINETICS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; STRUCTURE-ACTIVITY RELATIONSHIP; THERMODYNAMICS;

EID: 0031027579     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.4.2300     Document Type: Article

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