| pubmed-article:16140257 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16140257 | lifeskim:mentions | umls-concept:C0016213 | lld:lifeskim |
| pubmed-article:16140257 | lifeskim:mentions | umls-concept:C0030054 | lld:lifeskim |
| pubmed-article:16140257 | lifeskim:mentions | umls-concept:C1705822 | lld:lifeskim |
| pubmed-article:16140257 | lifeskim:mentions | umls-concept:C0348011 | lld:lifeskim |
| pubmed-article:16140257 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:16140257 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:16140257 | lifeskim:mentions | umls-concept:C0075350 | lld:lifeskim |
| pubmed-article:16140257 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:16140257 | pubmed:dateCreated | 2005-9-26 | lld:pubmed |
| pubmed-article:16140257 | pubmed:abstractText | Styrene monooxygenase (SMO) from Pseudomonas putida S12 is a two-component flavoenzyme composed of the NADH-specific flavin reductase, SMOB, and FAD-specific styrene epoxidase, SMOA. Here, we report the cloning, and expression of native and histidine-tagged versions of SMOA and SMOB and studies of the flavin transfer and styrene oxygenation reactions. In the reductive half-reaction, SMOB catalyzes the two-electron reduction of FAD with a turnover number of 3200 s(-1). Single turnover studies of the reaction of reduced SMOA with substrates indicate the formation of a stable oxygen intermediate with the absorbance characteristics of a flavin hydroperoxide. Based on the results of numerical simulations of the steady-state mechanism of SMO, we find that the observed coupling of NADH and styrene oxidation can be best explained by a model, which includes both the direct transfer and passive diffusion of reduced FAD from SMOB to SMOA. | lld:pubmed |
| pubmed-article:16140257 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16140257 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16140257 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16140257 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:16140257 | pubmed:issn | 0003-9861 | lld:pubmed |
| pubmed-article:16140257 | pubmed:author | pubmed-author:NguyenTimT | lld:pubmed |
| pubmed-article:16140257 | pubmed:author | pubmed-author:KantzAuricA | lld:pubmed |
| pubmed-article:16140257 | pubmed:author | pubmed-author:ChinFranklinF | lld:pubmed |
| pubmed-article:16140257 | pubmed:author | pubmed-author:NallamothuNag... | lld:pubmed |
| pubmed-article:16140257 | pubmed:author | pubmed-author:GassnerGeorge... | lld:pubmed |
| pubmed-article:16140257 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16140257 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:16140257 | pubmed:volume | 442 | lld:pubmed |
| pubmed-article:16140257 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16140257 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16140257 | pubmed:pagination | 102-16 | lld:pubmed |
| pubmed-article:16140257 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:16140257 | pubmed:meshHeading | pubmed-meshheading:16140257... | lld:pubmed |
| pubmed-article:16140257 | pubmed:meshHeading | pubmed-meshheading:16140257... | lld:pubmed |
| pubmed-article:16140257 | pubmed:meshHeading | pubmed-meshheading:16140257... | lld:pubmed |
| pubmed-article:16140257 | pubmed:meshHeading | pubmed-meshheading:16140257... | lld:pubmed |
| pubmed-article:16140257 | pubmed:year | 2005 | lld:pubmed |
| pubmed-article:16140257 | pubmed:articleTitle | Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase. | lld:pubmed |
| pubmed-article:16140257 | pubmed:affiliation | Department of Chemistry and Biochemistry, San Francisco State University, San Francisco, CA 94132-4163, USA. | lld:pubmed |
| pubmed-article:16140257 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16140257 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:16140257 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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