Glutamate residues at positions 219 and 252 in the α-subunit of the Escherichia coli ATP synthase are not functionally equivalent

Biochimica et Biophysica Acta - Bioenergetics

Volumn 1363, Issue 3, 1998, Pages 217-223

  Hatch, Lyndall P ^a   Cox, Graeme B ^a   Howitt, Susan M ^a  

^a AUSTRALIAN NATIONAL UNIVERSITY   (Australia)

Author keywords

ATP synthase; ATPase, F0F1 ; Proton translocation; Site directed mutagenesis

Indexed keywords

PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

AMINO ACID COMPOSITION; ARTICLE; ENZYME ACTIVITY; ENZYME SUBUNIT; ESCHERICHIA COLI; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

CELL MEMBRANE; COMPUTER SIMULATION; ESCHERICHIA COLI; GLUTAMIC ACID; MUTAGENESIS, SITE-DIRECTED; PROTON-TRANSLOCATING ATPASES;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0032565131     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0005-2728(97)00101-1     Document Type: Article

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