The purification of ammonia monooxygenase from Paracoccus denitrificans.

Abstract:

:The heterotrophic nitrifier Paracoccus denitrificans expresses a membrane-associated ammonia monooxygenase. The active enzyme has been solubilized in the detergent dodecyl-beta-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).

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Moir JW,Crossman LC,Spiro S,Richardson DJ

doi

10.1016/0014-5793(96)00463-2

subject

Has Abstract

pub_date

1996-05-27 00:00:00

pages

71-4

issue

1

eissn

0014-5793

issn

1873-3468

pii

0014579396004632

journal_volume

387

pub_type

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