Cross-linking of the δ subunit to one of the three α subunits has no effect on functioning, as expected if δ is a part of the stator that links the F1 and F0 parts of the Escherichia coli ATP synthase

Journal of Biological Chemistry

Volumn 272, Issue 26, 1997, Pages 16652-16656

  Ogilvie, Isla ^a   Aggeler, Robert ^a   Capaldi, Roderick A ^a  

^a UNIVERSITY OF OREGON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

N ETHYLMALEIMIDE; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ALPHA CHAIN; ALPHA HELIX; ARTICLE; CELL FUNCTION; CHLOROPLAST; COMPLEX FORMATION; CROSS LINKING; DISULFIDE BOND; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROTON TRANSPORT;

ADENOSINE TRIPHOSPHATE; COPPER; ESCHERICHIA COLI; PROTON-TRANSLOCATING ATPASES; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI; STATOR;

EID: 0030959251     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.272.26.16652     Document Type: Article

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