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The primary structure of cytochrome P460 of Nitrosomonas europaea : Presence of a c ‐heme binding motif
Author(s) -
Bergmann David J.,
Hooper Alan B.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)01072-2
Subject(s) - nitrosomonas europaea , heme , cytochrome , biochemistry , oxidoreductase , cytochrome c , chemistry , peptide sequence , cytochrome c peroxidase , cytochrome p450 reductase , stereochemistry , biology , coenzyme q – cytochrome c reductase , gene , enzyme , mitochondrion , nitrite , organic chemistry , nitrate
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.