The stalk region of the Escherichia coli ATP synthase: Tyrosine 205 of the γ subunit is in the interface between the F 1 and F 0 parts and can interact with both the ε and c oligomer

Journal of Biological Chemistry

Volumn 271, Issue 45, 1996, Pages 28341-28347

  Watts, Spencer D ^a   Tang, Chunlin ^a   Capaldi, Roderick A ^a  

^a UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ALPHA CHAIN; ARTICLE; COVALENT BOND; CROSS LINKING; ENZYME ACTIVITY; ENZYME MODIFICATION; ENZYME RECONSTITUTION; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROLYSIS; MEMBRANE BINDING; NONHUMAN; OXIDATIVE PHOSPHORYLATION; PRIORITY JOURNAL;

ADENYLYL IMIDODIPHOSPHATE; CYSTINE; DISULFIDES; DITHIONITROBENZOIC ACID; ESCHERICHIA COLI; MAGNESIUM; MALEIMIDES; PROTEIN CONFORMATION; PROTON-TRANSLOCATING ATPASES; TYROSINE;

ESCHERICHIA COLI;

EID: 0029854749     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.45.28341     Document Type: Article

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