Mutations in the dimerization domain of the b subunit from the Escherichia coli ATP synthase: Deletions disrupt function but not enzyme assembly

Journal of Biological Chemistry

Volumn 281, Issue 18, 2006, Pages 12408-12413

  Cipriano, Daniel J ^a   Wood, Kristi S ^a   Bi, Yumin ^a   Dunn, Stanley D ^a  

^a UNIVERSITY OF WESTERN ONTARIO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CATALYSIS; CELL MEMBRANES; DIMERIZATION; ESCHERICHIA COLI; MUTAGENESIS;

ACETATE; BINDING ANALYSES; ENERGY COUPLING; OXIDATIVE PHOSPHORYLATION;

ENZYMES;

ACETIC ACID; ALANINE; DICYCLOHEXYLCARBODIIMIDE; LYSINE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ARTICLE; BETA CHAIN; BINDING ASSAY; CONTROLLED STUDY; CROSS LINKING; DIMERIZATION; ENZYME ACTIVITY; ENZYME BINDING; ESCHERICHIA COLI; MISSENSE MUTATION; MUTAGENESIS; MUTATIONAL ANALYSIS; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PLASMID; PRIORITY JOURNAL; SEDIMENTATION;

AMINO ACID SEQUENCE; BACTERIAL PROTON-TRANSLOCATING ATPASES; BASE SEQUENCE; CROSS-LINKING REAGENTS; DIMERIZATION; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTAGENESIS, SITE-DIRECTED; MUTATION; PHOSPHORYLATION; PLASMIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY;

ESCHERICHIA COLI;

EID: 33744949445     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M513368200     Document Type: Article

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