The purification of ammonia monooxygenase from Paracoccus denitrificans

Moir, James W.B., Crossman, Lisa C., Spiro, Stephen and Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 (1996) The purification of ammonia monooxygenase from Paracoccus denitrificans. FEBS Letters, 387 (1). pp. 71-74. ISSN 0014-5793

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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).

Item Type: Article
Additional Information: Funding Information: grant GRI the EPSRC
Uncontrolled Keywords: ammonia monooxygenase,heterotrophic nitrification,paracoccus denitrificans,particulate methane monooxygenase,biophysics,structural biology,biochemistry,molecular biology,genetics,cell biology ,/dk/atira/pure/subjectarea/asjc/1300/1304
Faculty \ School: Faculty of Science > School of Biological Sciences
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Depositing User: LivePure Connector
Date Deposited: 14 Jul 2022 17:30
Last Modified: 12 Aug 2022 05:35
URI: https://ueaeprints.uea.ac.uk/id/eprint/86141
DOI: 10.1016/0014-5793(96)00463-2

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