Affordable Access

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

Authors
  • Bergmann, D J
  • Hooper, A B
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
Oct 24, 1994
Volume
353
Issue
3
Pages
324–326
Identifiers
PMID: 7957885
Source
Medline
License
Unknown

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.

Report this publication

Statistics

Seen <100 times