PMID:11321583
| Citation |
Rothery, RA, Blasco, F, Magalon, A and Weiner, JH (2001) The diheme cytochrome b subunit (Narl) of Escherichia coli nitrate reductase A (NarGHI): structure, function, and interaction with quinols. J. Mol. Microbiol. Biotechnol. 3:273-83 |
|---|---|
| Abstract |
Significant recent advances have been made in studies of the major dissimilatory nitrate reductase (NarGHI) of Escherichia coli. This enzyme is a complex iron-sulfur ([Fe-S]) molybdoenzyme that oxidizes menaquinol or ubiquinol at a periplasmically oriented Q-site (Qp site), and reduces nitrate at a cytoplasmically-oriented molybdo-(bismolybdopterin guanine dinucleotide) (Mo-bisMGD) cofactor. The Qp site, as well as two hemes, termed bL and bH, are localized in a hydrophobic diheme cytochrome b(Narl) that: (i) provides a conduit for electron-transfer from the periplasmically-oriented Qp-site; (ii) provides a membrane anchoring functionality for the membrane-extrinsic subunits (NarGH) that coordinate the Mo-bisMGD (NarG) and four [Fe-S] clusters (NarH); and (iii) helps ensure the separation of sites of H+-yielding and H+-consuming reactions such that enzyme turnover leads to the generation of a proton-electrochemical potential across the cytoplasmic membrane. This minireview focuses on recent advances and future prospects for the diheme cytochrome b subunit (Narl) of NarGHI. |
| Links | |
| Keywords |
Amino Acid Sequence; Cytochrome b Group/chemistry; Cytochrome b Group/genetics; Cytochrome b Group/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Guanine Nucleotides/metabolism; Heme/metabolism; Hydroquinones/metabolism; Models, Molecular; Molecular Sequence Data; Molybdenum/metabolism; Nitrate Reductase; Nitrate Reductases/chemistry; Nitrate Reductases/genetics; Nitrate Reductases/metabolism; Organometallic Compounds/metabolism; Protein Structure, Secondary; Protein Subunits; Sequence Alignment; Sequence Homology, Amino Acid |
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