The purification of ammonia monooxygenase from Paracoccus denitrificans

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

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105 Citations (Scopus)

Abstract

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).

Original languageEnglish
Pages (from-to)71-74
Number of pages4
JournalFEBS Letters
Volume387
Issue number1
DOIs
Publication statusPublished - 27 May 1996

Keywords

  • Ammonia monooxygenase
  • Heterotrophic nitrification
  • Paracoccus denitrificans
  • Particulate methane monooxygenase

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