The purification of ammonia monooxygenase from Paracoccus denitrficans

FEBS Letters

Spiro, Stephen¹  Crossman, Lisa C.¹  Moir, James W.B.¹  Richardson, David J.¹ 

[1] School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK

关键词: Ammonia monooxygenase;    Particulate methane monooxygenase;    Heterotrophic nitrification;    Paracoccus denitrificans;   

DOI  :  10.1016/0014-5793(96)00463-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The heterotrophic nitrifier Paracoccus denitrificans expresses a membrane-associated ammonia monooxygenase. The active enzyme has been solubilized in the detergent dodecyl-β-d-maltoside and purified by standard chromatographic techniques. This is the first purification of an ammonia monooxygenase. The enzyme consists of two subunits with molecular masses of 38 and 46 kDa. The purified enzyme is a quinol oxidase, is inhibited by light and a variety of chelating agents and is activated by cupric ions. These properties indicate that this enzyme has similarities to a family of enzymes including the ammonia monooxygenase from Nitrosomonas europaea and the particulate methane monooxygenase from Methylococcus capsulatus (Bath).

【 授权许可】

Unknown