Gene fusions with β-lactamase show that subunit I of the cytochrome bd quinol oxidase from E. coli has nine transmembrane helices with the O 2 reactive site near the periplasmic surface

FEBS Letters

Volumn 561, Issue 1-3, 2004, Pages 58-62

  Zhang, Jie ^a   Barquera, Blanca ^a   Gennis, Robert B ^a  

^a UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

Author keywords

Lactamase; Cytochrome bd; Gene fusion; Membrane protein; Oxidase; Topology

Indexed keywords

BACTERIAL ENZYME; BETA LACTAMASE; CYTOCHROME BD QUINOL OXIDASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

ARTICLE; CELL SURFACE; CYTOPLASM; ENZYME SUBUNIT; GENE FUSION; NONHUMAN; PRIORITY JOURNAL;

ARTIFICIAL GENE FUSION; BASE SEQUENCE; BETA-LACTAMASES; BINDING SITES; CYTOCHROMES; ELECTRON TRANSPORT CHAIN COMPLEX PROTEINS; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; OXIDOREDUCTASES; OXYGEN; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; RECOMBINANT FUSION PROTEINS;

ESCHERICHIA COLI; PROKARYOTA;

EID: 1542346467     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(04)00125-5     Document Type: Article

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