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FEBS Lett. 1994 Oct 24;353(3):324-6.

The primary structure of cytochrome P460 of Nitrosomonas europaea: presence of a c-heme binding motif.

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  • 1Graduate Program in Biochemistry, University of Minnesota, St. Paul 55108.

Abstract

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.

PMID:
7957885
[PubMed - indexed for MEDLINE]
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