EPR study of NO complex of bd-type ubiquinol oxidase from Escherichia coli: The proximal axial ligand of heme d is a nitrogenous amino acid residue

Journal of Biological Chemistry

Volumn 271, Issue 16, 1996, Pages 9254-9258

  Hori, Hiroshi ^a   Tsubaki, Motonari ^b   Mogil, Tatsushi ^c   Anraku, Yasuhiro ^c  

^a OSAKA UNIVERSITY   (Japan)

^b UNIVERSITY OF HYOGO   (Japan)

^c UNIVERSITY OF TOKYO   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

AMINO ACID; BACTERIAL ENZYME; CYTOCHROME C OXIDASE; HEME; HISTIDINE; LIGAND; NITRIC OXIDE; UBIQUINOL CYTOCHROME C REDUCTASE;

AEROBIC METABOLISM; ARTICLE; ELECTRON SPIN RESONANCE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RESPIRATORY CHAIN;

BINDING SITES; CYTOCHROME A GROUP; CYTOCHROME B GROUP; CYTOCHROME D GROUP; CYTOCHROMES; CYTOCHROMES A1; ELECTRON SPIN RESONANCE SPECTROSCOPY; ELECTRON TRANSPORT CHAIN COMPLEX PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEME; HISTIDINE; KINETICS; LIGANDS; NITRIC OXIDE; OXIDOREDUCTASES;

EID: 0029942493     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.271.16.9254     Document Type: Article

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