Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
47
pubmed:dateCreated
1994-1-10
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12928-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Quinoline oxidoreductase from Pseudomonas putida 86: an improved purification procedure and electron paramagnetic resonance spectroscopy.
pubmed:affiliation
Fachrichtung Biophysik und Physikalische Grundlagen der Medizin, Universität des Saarlandes, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't