Source:http://linkedlifedata.com/resource/pubmed/id/19228194
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2009-3-12
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pubmed:abstractText |
The chlorite dismutase (Cld) of Pseudomonas chloritidismutans was purified from the periplasmic fraction in one step by hydroxyapatite chromatography. The enzyme has a molecular mass of 110 kDa and consists of four 31-kDa subunits. Enzyme catalysis followed Michaelis-Menten kinetics, with Vmax and K(m) values of 443 U mg(-1) and 84 microM, respectively. A pyridine-NaOH-dithionite-reduced Cld revealed a Soret peak at 418 nm, indicative for protoheme IX. The spectral data indicate the presence of 1.5 mol protoheme IX mol(-1) tetrameric enzyme while metal analysis revealed 2.2 mol iron mol(-1) tetrameric enzyme. High concentrations of chlorite resulted in the disappearance of the Soret peak, which coincided with loss in activity. Electron paramagnetic resonance analyses showed an axial high-spin ferric iron signal. Cld was inhibited by cyanide, azide, but not by hydroxylamine or 3-amino-1,2,3-triazole. Remarkably, the activity was drastically enhanced by kosmotropic salts, and chaotropic salts decreased the activity, in accordance with the Hofmeister series. Chlorite conversion in the presence of 18O-labeled water did not result in the formation of oxygen with a mass of 34 (16O-18O) or a mass of 36 ((18)O-(18)O), indicating that water is not a substrate in the reaction and that both oxygen atoms originate from chlorite.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
1574-6968
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
293
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-21
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pubmed:meshHeading |
pubmed-meshheading:19228194-Catalysis,
pubmed-meshheading:19228194-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:19228194-Heme,
pubmed-meshheading:19228194-Kinetics,
pubmed-meshheading:19228194-Oxidoreductases,
pubmed-meshheading:19228194-Periplasm,
pubmed-meshheading:19228194-Pseudomonas,
pubmed-meshheading:19228194-Salts
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pubmed:year |
2009
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pubmed:articleTitle |
Purification and characterization of a chlorite dismutase from Pseudomonas chloritidismutans.
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pubmed:affiliation |
Laboratory of Microbiology, Wageningen University, Dreijenplein, Wageningen, The Netherlands.
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pubmed:publicationType |
Journal Article
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