The primary structure of cytochrome P460 of Nitrosomonas europaea: presence of a c-heme binding motif.
Cytochrome P460 and hydroxyamine oxidoreductase of Nitrosomonas europaea both catalyze the oxidation of hydroxylamine and contain a 460 nm-absorbing chromophore. The gene (cyp) encoding cytochrome P460 was cloned and sequenced. The predicted amino acid sequence contains a single c-heme binding motif (CXXCH) near the carboxy-terminus. Cytochrome P460 shows little sequence homology to other c-cytochromes including hydroxyamine oxidoreductase. The presence of a signal peptide and a possible c-heme binding site suggest that the cytochrome P460 of N. europaea is periplasmic.
Graduate Program in Biochemistry, University of Minnesota, St. Paul 55108.
D J
DJ
Bergmann
A B
AB
Hooper
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003580:Cytochromes / Q000235:genetics*; D005798:Genes, Bacterial / Q000235:genetics*; D006418:Heme / Q000031:analogs & derivatives* / Q000235:genetics; D008969:Molecular Sequence Data; D009606:Nitrosomonas / Q000201:enzymology / Q000235:genetics*; D017422:Sequence Analysis, DNA
D003580:Cytochromes; C031690:heme C; D006418:Heme; C080650:cytochrome P-460