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Chlorite dismutase from Ideonella dechloratans
Karlstad University, Division for Chemistry.
Karlstad University, Division for Chemistry.
Karlstad University, Division for Chemistry.
Department of Molecular Biotechnology, Chalmers University of Technology, Lundberg Laboratory.
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2001 (English)In: Journal of Biological Inorganic Chemistry, ISSN 0949-8257, E-ISSN 1432-1327, J Biol Inorg Chem 2001 June;5 (5-6):601-7, Vol. 6, no 5-6, p. 601-607Article in journal (Refereed) Published
Abstract [en]

Chlorite dismutase has been purified from the chlorate-metabolizing bacterium Ideonella dechloratans. The purified enzyme is tetrameric, with a relative molecular mass of 25,000 for the subunit, and contains about 0.6 heme/subunit as isolated. Its catalytic properties are similar, but not identical, to those found for a similar enzyme purified earlier from the bacterium GR-1. The heme group in Ideonella chlorite dismutase is readily reduced by dithionite, in contrast to the GR-1 enzyme, and redox titration gave a value of -21 mV for the midpoint potential at pH 7. The heme group has been characterized by optical and EPR spectroscopy. It is high-spin ferric at neutral pH, with spectroscopic properties similar to those found for cytochrome c peroxidase. In the alkaline pH range, a low-spin compound is formed. A 22-residue N-terminal amino acid sequence has been determined and no homologue has been found in the protein sequence databases.

Place, publisher, year, edition, pages
2001. Vol. 6, no 5-6, p. 601-607
National Category
Inorganic Chemistry
Research subject
Chemistry
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URN: urn:nbn:se:kau:diva-17681DOI: 10.1007/s007750100237PubMedID: 11472023OAI: oai:DiVA.org:kau-17681DiVA, id: diva2:591293
Available from: 2013-01-21 Created: 2013-01-21 Last updated: 2017-12-06Bibliographically approved

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Nilsson, Thomas

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