The γε-γ subunit interface in the ATP synthase of Escherichia coli. Cross-linking of the ε subunit to the c subunit ring does not impair enzyme function, that of γ to c subunits leads to uncoupling

Journal of Biological Chemistry

Volumn 274, Issue 48, 1999, Pages 34233-34237

  Schulenberg, Birte ^a   Aggeler, Robert ^a   Murray, James ^a   Capaldi, Roderick A ^a  

^a UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACRIDINE DERIVATIVE; ADENOSINE TRIPHOSPHATE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; COPPER; CROSS LINKING REAGENT; CUPROUS CHLORIDE; PEPTIDE FRAGMENT; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATASE;

ARTICLE; CONFORMATIONAL TRANSITION; CROSS LINKING; ENZYME ACTIVITY; ENZYME CONFORMATION; ENZYME SUBUNIT; ESCHERICHIA COLI; GENE MUTATION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT; SYNTHESIS; AMINO ACID SUBSTITUTION; BINDING SITE; CHEMISTRY; DRUG EFFECT; ENZYME ACTIVATION; ENZYMOLOGY; GENETICS; METABOLISM; MUTATION; SITE DIRECTED MUTAGENESIS;

AMINO ACID SUBSTITUTION; BINDING SITES; COPPER; CROSS-LINKING REAGENTS; ENZYME ACTIVATION; ESCHERICHIA COLI; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDE FRAGMENTS; PROTON-TRANSLOCATING ATPASES;

EID: 0033607324     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.48.34233     Document Type: Article

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