| pubmed-article:18652479 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18652479 | lifeskim:mentions | umls-concept:C0205103 | lld:lifeskim |
| pubmed-article:18652479 | lifeskim:mentions | umls-concept:C0016223 | lld:lifeskim |
| pubmed-article:18652479 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:18652479 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
| pubmed-article:18652479 | lifeskim:mentions | umls-concept:C0242417 | lld:lifeskim |
| pubmed-article:18652479 | lifeskim:mentions | umls-concept:C2604343 | lld:lifeskim |
| pubmed-article:18652479 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:18652479 | pubmed:dateCreated | 2008-8-12 | lld:pubmed |
| pubmed-article:18652479 | pubmed:abstractText | This work describes for the first time the identification of a reaction intermediate, C4a-hydroperoxyflavin, during the oxidative half-reaction of a flavoprotein oxidase, pyranose 2-oxidase (P2O) from Trametes multicolor, by using rapid kinetics. The reduced P2O reacted with oxygen with a forward rate constant of 5.8 x 10 (4) M (-1) s (-1) and a reverse rate constant of 2 s (-1), resulting in the formation of a C4a-hydroperoxyflavin intermediate which decayed with a rate constant of 18 s (-1). The absorption spectrum of the intermediate resembled the spectra of flavin-dependent monooxygenases. A hydrophobic cavity formed at the re side of the flavin ring in the closed state structure of P2O may help in stabilizing the intermediate. | lld:pubmed |
| pubmed-article:18652479 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18652479 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18652479 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18652479 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18652479 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18652479 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18652479 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18652479 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18652479 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18652479 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:18652479 | pubmed:author | pubmed-author:HaltrichDietm... | lld:pubmed |
| pubmed-article:18652479 | pubmed:author | pubmed-author:ChaiyenPimcha... | lld:pubmed |
| pubmed-article:18652479 | pubmed:author | pubmed-author:SucharitakulJ... | lld:pubmed |
| pubmed-article:18652479 | pubmed:author | pubmed-author:ProngjitMethi... | lld:pubmed |
| pubmed-article:18652479 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18652479 | pubmed:day | 19 | lld:pubmed |
| pubmed-article:18652479 | pubmed:volume | 47 | lld:pubmed |
| pubmed-article:18652479 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18652479 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18652479 | pubmed:pagination | 8485-90 | lld:pubmed |
| pubmed-article:18652479 | pubmed:dateRevised | 2011-4-6 | lld:pubmed |
| pubmed-article:18652479 | pubmed:meshHeading | pubmed-meshheading:18652479... | lld:pubmed |
| pubmed-article:18652479 | pubmed:meshHeading | pubmed-meshheading:18652479... | lld:pubmed |
| pubmed-article:18652479 | pubmed:meshHeading | pubmed-meshheading:18652479... | lld:pubmed |
| pubmed-article:18652479 | pubmed:meshHeading | pubmed-meshheading:18652479... | lld:pubmed |
| pubmed-article:18652479 | pubmed:meshHeading | pubmed-meshheading:18652479... | lld:pubmed |
| pubmed-article:18652479 | pubmed:meshHeading | pubmed-meshheading:18652479... | lld:pubmed |
| pubmed-article:18652479 | pubmed:meshHeading | pubmed-meshheading:18652479... | lld:pubmed |
| pubmed-article:18652479 | pubmed:meshHeading | pubmed-meshheading:18652479... | lld:pubmed |
| pubmed-article:18652479 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18652479 | pubmed:articleTitle | Detection of a C4a-hydroperoxyflavin intermediate in the reaction of a flavoprotein oxidase. | lld:pubmed |
| pubmed-article:18652479 | pubmed:affiliation | Department of Biochemistry, Faculty of Dentistry, Chulalongkorn University, Henri-Dunant Road, Patumwan, Bangkok 10300, Thailand. | lld:pubmed |
| pubmed-article:18652479 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18652479 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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