Source:http://linkedlifedata.com/resource/pubmed/id/17069757
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2006-11-30
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pubmed:abstractText |
Mycobacterium leprae GlbO has been proposed to represent merging of both O(2) uptake/transport and scavenging of nitrogen reactive species. Peroxynitrite reacts with M. leprae GlbO(II)-NO leading to GlbO(III) via the GlbO(III)-NO species. The value of the second order rate constant for GlbO(III)-NO formation is >1x10(8)M(-1)s(-1) in the absence and presence of CO(2) (1.2x10(-3)M). The CO(2)-independent value of the first order rate constant for GlbO(III)-NO denitrosylation is (2.5+/-0.4)x10(1)s(-1). Furthermore, peroxynitrite reacts with GlbO(II)-O(2) leading to GlbO(III) via the GlbO(IV)O species. Values of the second order rate constant for GlbO(IV)O formation are (4.8+/-0.5)x10(4) and (6.3+/-0.7)x10(5)M(-1)s(-1) in the absence and presence of CO(2) (=1.2x10(-3)M), respectively. The value of the second order rate constant for the peroxynitrite-mediated GlbO(IV)O reduction (= (1.5+/-0.2)x10(4)M(-1)s(-1)) is CO(2)-independent. These data argue for a role of GlbO in the defense of M. leprae against nitrosative stress.
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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/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Dioxide,
http://linkedlifedata.com/resource/pubmed/chemical/Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxynitrous Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Reactive Oxygen Species,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Truncated Hemoglobins,
http://linkedlifedata.com/resource/pubmed/chemical/truncated hemoglobin...
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
351
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
528-33
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:17069757-Bacterial Proteins,
pubmed-meshheading:17069757-Carbon Dioxide,
pubmed-meshheading:17069757-Hemoglobins,
pubmed-meshheading:17069757-Kinetics,
pubmed-meshheading:17069757-Mycobacterium leprae,
pubmed-meshheading:17069757-Oxidation-Reduction,
pubmed-meshheading:17069757-Peroxynitrous Acid,
pubmed-meshheading:17069757-Reactive Oxygen Species,
pubmed-meshheading:17069757-Recombinant Proteins,
pubmed-meshheading:17069757-Truncated Hemoglobins
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pubmed:year |
2006
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pubmed:articleTitle |
Peroxynitrite scavenging by ferrous truncated hemoglobin GlbO from Mycobacterium leprae.
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pubmed:affiliation |
National Institute for Infectious Diseases I.R.C.C.S. Lazzaro Spallanzani, Via Portuense 292, I-00149 Roma, Italy. ascenzi@bio.uniroma3.it
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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