The trapping of different conformations of the Escherichia coli F1 ATPase by disulfide bond formation: Effect on nucleotide binding affinities of the catalytic sites

Journal of Biological Chemistry

Volumn 271, Issue 51, 1996, Pages 32623-32628

  Grüber, Gerhard ^a   Capaldi, Roderick A ^a  

^a UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE;

ARTICLE; BINDING AFFINITY; BINDING COMPETITION; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME STRUCTURE; ESCHERICHIA COLI; PRIORITY JOURNAL;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BINDING SITES; CROSS-LINKING REAGENTS; DISULFIDES; EDETIC ACID; ESCHERICHIA COLI; MUTAGENESIS, SITE-DIRECTED; PROTEIN BINDING; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; SPECTRUM ANALYSIS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0030450752     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.51.32623     Document Type: Article

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