| pubmed-article:12644706 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C0027078 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C0332157 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C1323274 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C1875307 | lld:lifeskim |
| pubmed-article:12644706 | lifeskim:mentions | umls-concept:C0205154 | lld:lifeskim |
| pubmed-article:12644706 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:12644706 | pubmed:dateCreated | 2003-4-2 | lld:pubmed |
| pubmed-article:12644706 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:abstractText | A binding site for metal ions has been created on the surface of horse heart myoglobin (Mb) near the heme 6-propionate group by replacing K45 and K63 with glutamyl residues. One-dimensional (1)H NMR spectroscopy indicates that Mn(2+) binds in the vicinity of the heme 6-propionate as anticipated, and potentiometric titrations establish that the affinity of the new site for Mn(2+) is 1.28(4) x 10(4) M(-1) (pH 6.96, ionic strength I = 17.2 microM, 25 degrees C). In addition, these substitutions lower the reduction potential of the protein and increase the pK(a) for the water molecule coordinated to the heme iron of metmyoglobin. The peroxidase [2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid), ABTS, as substrate] and the Mn(2+)-peroxidase activity of the variant are both increased approximately 3-fold. In contrast to wild-type Mb, both the affinity for azide and the midpoint potential of the variant are significantly influenced by the addition of Mn(2+). The structure of the variant has been determined by x-ray crystallography to define the coordination environment of bound Mn(2+) and Cd(2+). Although slight differences are observed between the geometry of the binding of the two metal ions, both are hexacoordinate, and neither involves coordination by E63. | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12644706 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12644706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12644706 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12644706 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12644706 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:KiddA SAS | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:MaurusRobertR | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:BrayerGary... | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:SmithMichaelM | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:MaukA GrantAG | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:RavenEmma LEL | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:HunterChristi... | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:MaukMarcia... | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:TongHarryH | lld:pubmed |
| pubmed-article:12644706 | pubmed:author | pubmed-author:NguyenNhamN | lld:pubmed |
| pubmed-article:12644706 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12644706 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:12644706 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:12644706 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12644706 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12644706 | pubmed:pagination | 3647-52 | lld:pubmed |
| pubmed-article:12644706 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:meshHeading | pubmed-meshheading:12644706... | lld:pubmed |
| pubmed-article:12644706 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12644706 | pubmed:articleTitle | Introduction and characterization of a functionally linked metal ion binding site at the exposed heme edge of myoglobin. | lld:pubmed |
| pubmed-article:12644706 | pubmed:affiliation | Department of Biochemistry and Molecular Biology and Protein Engineering Network of Centres of Excellence, University of British Columbia, Vancouver, BC, Canada V6T 1Z3. | lld:pubmed |
| pubmed-article:12644706 | pubmed:publicationType | Journal Article | lld:pubmed |
