THE PRIMARY STRUCTURE OF CYTOCHROME P460 OF NITROSOMONAS-EUROPAEA - PRESENCE OF A C-HEME BINDING MOTIF

被引：25

作者：

BERGMANN, DJ ^{[1
]}

HOOPER, AB ^{[1
]}

机构：

[1] UNIV MINNESOTA,CTR BIOSCI 250,DEPT GENET & CELL BIOL,ST PAUL,MN 55108

来源：

FEBS LETTERS | 1994年 / 353卷 / 03期

基金：

美国国家科学基金会;

关键词：

AMMONIA OXIDATION; CYP; CYTOCHROME P460; HYDROXYLAMINE OXIDATION; NITROSOMONAS EUROPAEA;

D O I：

10.1016/0014-5793(94)01072-2

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：324 / 326

页数：3

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