| pubmed-article:17707766 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17707766 | lifeskim:mentions | umls-concept:C0026912 | lld:lifeskim |
| pubmed-article:17707766 | lifeskim:mentions | umls-concept:C0028128 | lld:lifeskim |
| pubmed-article:17707766 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
| pubmed-article:17707766 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:17707766 | lifeskim:mentions | umls-concept:C0108413 | lld:lifeskim |
| pubmed-article:17707766 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17707766 | pubmed:dateCreated | 2007-9-4 | lld:pubmed |
| pubmed-article:17707766 | pubmed:abstractText | CO dehydrogenase (CO-DH) catalyzes the oxidation of CO to CO(2) in carboxydobacteria. Cell-free extracts prepared from several mycobacteria, including Mycobacterium tuberculosis H37Ra, showed NO dehydrogenase (NO-DH) activity in a reaction mixture containing sodium nitroprusside (SNP) as the source of NO. The association of the NO-DH activity with CO-DH was revealed by activity staining and confirmed by enzyme assay with purified CO-DH from Mycobacterium sp. strain JC1, a carboxydotrophic mycobacterium. SNP stimulated the production of CO-DH with a coincidental increase in NO-DH activity in the bacterium, further supporting this association and implying the existence of a possible SNP-induced CO-DH gene expression. The addition of purified CO-DH to cultures of Escherichia coli revealed that the enzyme protected E. coli from SNP-induced killing in a dose-dependant way. The present results indicate that mycobacterial CO-DH also acts as a NO-DH, which may function in the protection of mycobacterial pathogens from nitrosative stress during infection. | lld:pubmed |
| pubmed-article:17707766 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17707766 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17707766 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17707766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17707766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17707766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17707766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17707766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17707766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17707766 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17707766 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17707766 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:17707766 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:17707766 | pubmed:author | pubmed-author:EomChi-YongCY | lld:pubmed |
| pubmed-article:17707766 | pubmed:author | pubmed-author:OhJeong-IlJI | lld:pubmed |
| pubmed-article:17707766 | pubmed:author | pubmed-author:KimYoung... | lld:pubmed |
| pubmed-article:17707766 | pubmed:author | pubmed-author:KimEungbinE | lld:pubmed |
| pubmed-article:17707766 | pubmed:author | pubmed-author:SongTaeksunT | lld:pubmed |
| pubmed-article:17707766 | pubmed:author | pubmed-author:KimSeo... | lld:pubmed |
| pubmed-article:17707766 | pubmed:author | pubmed-author:ParkSae... | lld:pubmed |
| pubmed-article:17707766 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17707766 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:17707766 | pubmed:volume | 362 | lld:pubmed |
| pubmed-article:17707766 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17707766 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17707766 | pubmed:pagination | 449-53 | lld:pubmed |
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| pubmed-article:17707766 | pubmed:meshHeading | pubmed-meshheading:17707766... | lld:pubmed |
| pubmed-article:17707766 | pubmed:meshHeading | pubmed-meshheading:17707766... | lld:pubmed |
| pubmed-article:17707766 | pubmed:meshHeading | pubmed-meshheading:17707766... | lld:pubmed |
| pubmed-article:17707766 | pubmed:meshHeading | pubmed-meshheading:17707766... | lld:pubmed |
| pubmed-article:17707766 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17707766 | pubmed:articleTitle | Carbon monoxide dehydrogenase in mycobacteria possesses a nitric oxide dehydrogenase activity. | lld:pubmed |
| pubmed-article:17707766 | pubmed:affiliation | Department of Biology, Yonsei University, Seoul 120-749, Republic of Korea. | lld:pubmed |
| pubmed-article:17707766 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17707766 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17707766 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17707766 | lld:pubmed |
