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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
47
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pubmed:dateCreated |
1994-1-10
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pubmed:abstractText |
Quinoline oxidoreductase, an iron-sulfur molybdenum flavoprotein containing flavin adenine dinucleotide and molybdopterin cytosine dinucleotide, was purified from Pseudomonas putida 86 to homogeneity. The various electron-transfer centers of the purified enzyme were examined by electron paramagnetic resonance spectroscopy. Quinoline deuterated at position 2 was prepared by deuterodecarboxylation of 2-quinolinecarboxylic acid. Quinoline added to the enzyme elicited the Mo(V) "rapid" type Q signal arising from the complex of enzyme and substrate, whereas in oxidized quinoline oxidoreductase a Mo(V) "resting" signal was observed. EPR spectroscopy at helium temperatures below 70 K revealed the existence of two types of iron-sulfur centers, Fe-S I and Fe-S II. An organic free radical appeared upon reduction with sodium dithionite. Inactivation of the enzyme by cyanide led to the inactive desulfo quinoline oxidoreductase, which yielded another Mo(V) signal designated "slow" type Q upon reduction with dithionite. Desulfo quinoline oxidoreductase was partially reactivated by incubation with sulfide.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cyanides,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Reactivators,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Molybdenum,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on CH-CH...,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfides,
http://linkedlifedata.com/resource/pubmed/chemical/quinoline 2-oxidoreductase,
http://linkedlifedata.com/resource/pubmed/chemical/sodium sulfide
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12928-34
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8251516-Cyanides,
pubmed-meshheading:8251516-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:8251516-Enzyme Reactivators,
pubmed-meshheading:8251516-Free Radicals,
pubmed-meshheading:8251516-Iron-Sulfur Proteins,
pubmed-meshheading:8251516-Molybdenum,
pubmed-meshheading:8251516-Oxidation-Reduction,
pubmed-meshheading:8251516-Oxidoreductases,
pubmed-meshheading:8251516-Oxidoreductases Acting on CH-CH Group Donors,
pubmed-meshheading:8251516-Pseudomonas putida,
pubmed-meshheading:8251516-Sulfides
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pubmed:year |
1993
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pubmed:articleTitle |
Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy.
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pubmed:affiliation |
Fachrichtung Biophysik und Physikalische Grundlagen der Medizin, Universität des Saarlandes, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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