The diheme cytochrome b subunit (Narl) of Escherichia coli nitrate reductase A (NarGHI): Structure, function, and interaction with quinols

Journal of Molecular Microbiology and Biotechnology

Volumn 3, Issue 2, 2001, Pages 273-283

  Rothery, Richard A ^a   Blasco, Francis ^b   Magalon, Axel ^c   Weiner, Joel H ^a  

^a UNIVERSITY OF ALBERTA   (Canada)

^b CNRS   (France)

^c UNIVERSITY OF MUNICH   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CYTOCHROME B; HEME; IRON SULFUR PROTEIN; MENAQUINONE; MOLYBDENUM IRON PROTEIN; NITRATE; NITRATE REDUCTASE; PROTEIN SUBUNIT; UBIQUINONE;

AMINO ACID SEQUENCE; BINDING SITE; CYTOPLASM; ELECTRON SPIN RESONANCE; ELECTRON TRANSPORT; ENZYME ACTIVITY; ENZYME BINDING; ENZYME CONFORMATION; ENZYME LOCALIZATION; ENZYME STRUCTURE; ENZYME SUBUNIT; ESCHERICHIA COLI; GENE OVEREXPRESSION; GENE SEQUENCE; HYDROPHOBICITY; NONHUMAN; PROTON MOTIVE FORCE; REVIEW; SEQUENCE ANALYSIS; SITE DIRECTED MUTAGENESIS;

AMINO ACID SEQUENCE; CYTOCHROME B GROUP; ESCHERICHIA COLI; GUANINE NUCLEOTIDES; HEME; HYDROQUINONES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLYBDENUM; NITRATE REDUCTASE; NITRATE REDUCTASES; ORGANOMETALLIC COMPOUNDS; PROTEIN STRUCTURE, SECONDARY; PROTEIN SUBUNITS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID;

ESCHERICHIA COLI;

EID: 0035088582     PISSN: 14641801     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

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