The primary structure of cytochrome P460 of Nitrosomonas europaea: Presence of a c‐heme binding motif

FEBS Letters

Hooper, Alan B.¹  Bergmann, David J.¹ 

[1]Graduate Program in Biochemistry, and Department of Genetics and Cell Biology, Univerity of Minnesota, St. Paul, MN 55108, USA

关键词: Ammonia oxidation;    cyp;    Cytochrome P460;    Hydroxylamine oxidation;    Nitrosomonas europaea;   

DOI  :  10.1016/0014-5793(94)01072-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown