| pubmed-article:21261288 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21261288 | lifeskim:mentions | umls-concept:C0521009 | lld:lifeskim |
| pubmed-article:21261288 | lifeskim:mentions | umls-concept:C0031456 | lld:lifeskim |
| pubmed-article:21261288 | lifeskim:mentions | umls-concept:C1705920 | lld:lifeskim |
| pubmed-article:21261288 | lifeskim:mentions | umls-concept:C0007382 | lld:lifeskim |
| pubmed-article:21261288 | lifeskim:mentions | umls-concept:C1511572 | lld:lifeskim |
| pubmed-article:21261288 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:21261288 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:21261288 | pubmed:dateCreated | 2011-3-15 | lld:pubmed |
| pubmed-article:21261288 | pubmed:abstractText | Phenylalanine hydroxylase is a mononuclear non-heme iron protein that uses tetrahydropterin as the source of the two electrons needed to activate dioxygen for the hydroxylation of phenylalanine to tyrosine. Rapid-quench methods have been used to analyze the mechanism of a bacterial phenylalanine hydroxylase from Chromobacterium violaceum. Mo?ssbauer spectra of samples prepared by freeze-quenching the reaction of the enzyme-(57)Fe(II)-phenylalanine-6-methyltetrahydropterin complex with O(2) reveal the accumulation of an intermediate at short reaction times (20-100 ms). The Mo?ssbauer parameters of the intermediate (? = 0.28 mm/s, and |?E(Q)| = 1.26 mm/s) suggest that it is a high-spin Fe(IV) complex similar to those that have previously been detected in the reactions of other mononuclear Fe(II) hydroxylases, including a tetrahydropterin-dependent tyrosine hydroxylase. Analysis of the tyrosine content of acid-quenched samples from similar reactions establishes that the Fe(IV) intermediate is kinetically competent to be the hydroxylating intermediate. Similar chemical-quench analysis of a reaction allowed to proceed for several turnovers shows a burst of tyrosine formation, consistent with rate-limiting product release. All three data sets can be modeled with a mechanism in which the enzyme-substrate complex reacts with oxygen to form an Fe(IV)?O intermediate with a rate constant of 19 mM(-1) s(-1), the Fe(IV)?O intermediate hydroxylates phenylalanine with a rate constant of 42 s(-1), and rate-limiting product release occurs with a rate constant of 6 s(-1) at 5 °C. | lld:pubmed |
| pubmed-article:21261288 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21261288 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21261288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21261288 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21261288 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:21261288 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:21261288 | pubmed:author | pubmed-author:KrebsCarstenC | lld:pubmed |
| pubmed-article:21261288 | pubmed:author | pubmed-author:LeeMichaelM | lld:pubmed |
| pubmed-article:21261288 | pubmed:author | pubmed-author:FitzpatrickPa... | lld:pubmed |
| pubmed-article:21261288 | pubmed:author | pubmed-author:BollingerJ... | lld:pubmed |
| pubmed-article:21261288 | pubmed:author | pubmed-author:PanayAram... | lld:pubmed |
| pubmed-article:21261288 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21261288 | pubmed:day | 22 | lld:pubmed |
| pubmed-article:21261288 | pubmed:volume | 50 | lld:pubmed |
| pubmed-article:21261288 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21261288 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21261288 | pubmed:pagination | 1928-33 | lld:pubmed |
| pubmed-article:21261288 | pubmed:meshHeading | pubmed-meshheading:21261288... | lld:pubmed |
| pubmed-article:21261288 | pubmed:meshHeading | pubmed-meshheading:21261288... | lld:pubmed |
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| pubmed-article:21261288 | pubmed:meshHeading | pubmed-meshheading:21261288... | lld:pubmed |
| pubmed-article:21261288 | pubmed:meshHeading | pubmed-meshheading:21261288... | lld:pubmed |
| pubmed-article:21261288 | pubmed:meshHeading | pubmed-meshheading:21261288... | lld:pubmed |
| pubmed-article:21261288 | pubmed:meshHeading | pubmed-meshheading:21261288... | lld:pubmed |
| pubmed-article:21261288 | pubmed:meshHeading | pubmed-meshheading:21261288... | lld:pubmed |
| pubmed-article:21261288 | pubmed:meshHeading | pubmed-meshheading:21261288... | lld:pubmed |
| pubmed-article:21261288 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21261288 | pubmed:articleTitle | Evidence for a high-spin Fe(IV) species in the catalytic cycle of a bacterial phenylalanine hydroxylase. | lld:pubmed |
| pubmed-article:21261288 | pubmed:affiliation | Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843, United States. | lld:pubmed |
| pubmed-article:21261288 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21261288 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:21261288 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:21261288 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
