The transmembrane domain of subunit b of the Escherichia-coli F 1Fo ATP synthase is sufficient for H+- translocating activity together with subunits a and c

European Journal of Biochemistry

Volumn 271, Issue 14, 2004, Pages 3036-3042

  Greie, Jörg Christian ^a   Heitkamp, Thomas ^a   Altendorf, Karlheinz ^a  

^a UNIVERSITY OF OSNABRÜCK   (Germany)

Author keywords

Escherichia coli; F1Fo ATP synthase; Proton translocation; Reconstitution; Subunit b

Indexed keywords

DICYCLOHEXYLCARBODIIMIDE; HYDROGEN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE;

ALPHA CHAIN; ARTICLE; BACTERIAL TRANSLOCATION; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME SUBUNIT; ESCHERICHIA COLI; HYDROPHILICITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL;

BIOLOGICAL TRANSPORT; DICYCLOHEXYLCARBODIIMIDE; ESCHERICHIA COLI PROTEINS; LIPOSOMES; MACROMOLECULAR SUBSTANCES; MITOCHONDRIAL PROTON-TRANSLOCATING ATPASES; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEIN SUBUNITS; PROTONS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; JONES; NEGIBACTERIA;

EID: 3242781685     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04235.x     Document Type: Article

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