| pubmed-article:21110976 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21110976 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
| pubmed-article:21110976 | lifeskim:mentions | umls-concept:C0031760 | lld:lifeskim |
| pubmed-article:21110976 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:21110976 | lifeskim:mentions | umls-concept:C0015540 | lld:lifeskim |
| pubmed-article:21110976 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
| pubmed-article:21110976 | lifeskim:mentions | umls-concept:C0596335 | lld:lifeskim |
| pubmed-article:21110976 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:21110976 | pubmed:dateCreated | 2011-1-7 | lld:pubmed |
| pubmed-article:21110976 | pubmed:abstractText | The redox-midpoint potential of the FAD chromophore in the BLUF domain of anti-transcriptional regulator AppA from Rhodobacter sphaeroides equals ?-260mV relative to the calomel electrode. Altering the structure of its chromophore-binding pocket through site-directed mutagenesis brings this midpoint potential closer to that of free flavin in aqueous solution. The redox-midpoint potential of this BLUF domain is intermediate between those of LOV domains and Cryptochromes, which may rationalize the primary photochemistry observed in these three flavin-containing photoreceptor families. These results also imply that LOV domains, among the flavin-containing photosensory receptors, are least sensitive to intracellular chemical reduction in the dark. | lld:pubmed |
| pubmed-article:21110976 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21110976 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21110976 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21110976 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21110976 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:21110976 | pubmed:issn | 1873-3468 | lld:pubmed |
| pubmed-article:21110976 | pubmed:author | pubmed-author:HellingwerfKl... | lld:pubmed |
| pubmed-article:21110976 | pubmed:author | pubmed-author:HendriksJohnn... | lld:pubmed |
| pubmed-article:21110976 | pubmed:author | pubmed-author:ArentsJos CJC | lld:pubmed |
| pubmed-article:21110976 | pubmed:author | pubmed-author:PerezMarcela... | lld:pubmed |
| pubmed-article:21110976 | pubmed:copyrightInfo | Copyright © 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. | lld:pubmed |
| pubmed-article:21110976 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21110976 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:21110976 | pubmed:volume | 585 | lld:pubmed |
| pubmed-article:21110976 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21110976 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21110976 | pubmed:pagination | 167-72 | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
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| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
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| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:meshHeading | pubmed-meshheading:21110976... | lld:pubmed |
| pubmed-article:21110976 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21110976 | pubmed:articleTitle | On the midpoint potential of the FAD chromophore in a BLUF-domain containing photoreceptor protein. | lld:pubmed |
| pubmed-article:21110976 | pubmed:affiliation | Swammerdam Institute for Life Science, University of Amsterdam, Amsterdam, The Netherlands. | lld:pubmed |
| pubmed-article:21110976 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:3718631 | entrezgene:pubmed | pubmed-article:21110976 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21110976 | lld:entrezgene |
