Differentiation of catalytic sites on Escherichia coli F1ATPase by laser photoactivated labeling with [3H]-2-azido-ATP using the mutant βGlu381Cys:εSer108Cys to identify different β subunits by their interactions with γ and ε subunits

Biochemistry

Volumn 35, Issue 13, 1996, Pages

  Grüber, Gerhard ^a   Capaldi, Roderick A ^a  

^a UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

ADENOSINE TRIPHOSPHATASE;

ARTICLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBUNIT; ESCHERICHIA COLI; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PHOTOACTIVATION; PRIORITY JOURNAL;

ADENOSINE TRIPHOSPHATE; AFFINITY LABELS; AZIDES; CYSTEINE; EDETIC ACID; ESCHERICHIA COLI; GLUTAMIC ACID; KINETICS; MACROMOLECULAR SUBSTANCES; MAGNESIUM; MUTAGENESIS, SITE-DIRECTED; PHOTOLYSIS; POINT MUTATION; PROTEIN BINDING; PROTON-TRANSLOCATING ATPASES; RECOMBINANT PROTEINS; SERINE; SPECTROMETRY, FLUORESCENCE; TRITIUM;

EID: 5344261738     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi952949h     Document Type: Article

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