| pubmed-article:15044098 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15044098 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:15044098 | lifeskim:mentions | umls-concept:C0219010 | lld:lifeskim |
| pubmed-article:15044098 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:15044098 | pubmed:dateCreated | 2004-3-26 | lld:pubmed |
| pubmed-article:15044098 | pubmed:abstractText | The D-region connecting helices C and E of Vitreoscilla hemoglobin (VHb) appears disordered in the crystal structure. Six site-directed mutants in this region were made to investigate its possible functions. The mutant VHb's were analyzed using UV-visible and FTIR spectroscopy, using primarily the CO liganded forms, and their heme/protein ratios were determined. The results implicate Asp44, Arg47, and Glu49 as especially important in heme-globin interactions and ligand binding, and enabled construction of a model in which the D-region forms a loop that protrudes upward over the heme. Interactions between VHb (wild type and the D-region mutants) with the flavin domain of 2,4-DNT dioxygenase from Burkholderia were tested using bacterial two-hybrid screening. There was a correlation between the extent of the D-loop perturbation predicted for each mutant and the amount of the reduction in VHb-flavin domain interaction, suggesting that this region may be more generally involved in binding of VHb to flavoproteins. | lld:pubmed |
| pubmed-article:15044098 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15044098 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15044098 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:15044098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15044098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15044098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15044098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15044098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15044098 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15044098 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15044098 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:15044098 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:15044098 | pubmed:author | pubmed-author:LeeSang... | lld:pubmed |
| pubmed-article:15044098 | pubmed:author | pubmed-author:WebsterDale... | lld:pubmed |
| pubmed-article:15044098 | pubmed:author | pubmed-author:StarkBenjamin... | lld:pubmed |
| pubmed-article:15044098 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15044098 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:15044098 | pubmed:volume | 316 | lld:pubmed |
| pubmed-article:15044098 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15044098 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15044098 | pubmed:pagination | 1101-6 | lld:pubmed |
| pubmed-article:15044098 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:15044098 | pubmed:meshHeading | pubmed-meshheading:15044098... | lld:pubmed |
| pubmed-article:15044098 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15044098 | pubmed:articleTitle | Structure-function studies of the Vitreoscilla hemoglobin D-region. | lld:pubmed |
| pubmed-article:15044098 | pubmed:affiliation | Biology Division, Department of Biological, Chemical, and Physical Sciences, Illinois Institute of Technology, Chicago, IL 60616, USA. | lld:pubmed |
| pubmed-article:15044098 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15044098 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:15044098 | pubmed:publicationType | Evaluation Studies | lld:pubmed |
| pubmed-article:15044098 | pubmed:publicationType | Validation Studies | lld:pubmed |
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