| pubmed-article:14514887 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C0449829 | lld:lifeskim |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C1883073 | lld:lifeskim |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C1533148 | lld:lifeskim |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:14514887 | lifeskim:mentions | umls-concept:C1705492 | lld:lifeskim |
| pubmed-article:14514887 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:14514887 | pubmed:dateCreated | 2003-10-15 | lld:pubmed |
| pubmed-article:14514887 | pubmed:abstractText | When low levels of gaseous nitric oxide (NO) are equilibrated with deoxygenated Hb, all NO added can be accounted for in terms of hexacoordinate and pentacoordinate forms of NO-Hb, despite recent reports on NO disappearance from heme groups to form nitroxyl anions or S-nitrosated Hb at low ratios of NO to Hb. We demonstrate that a fraction of the spectral signature of fully nitrosylated (largely hexacoordinate) Hb disappears as the pentacoordinate state forms and reappears when pentacoordinate NO-Hb is reconverted to the hexacoordinate condition. We show that the spectral changes associated with these reversible shifts in NO- heme geometry can be remarkably well approximated as variations in the contributions from fully nitrosylated Hb and oxidized Hb (MetHb). As a result, increases in the level of pentacoordinate NO-Hb that occur at low NO to Hb ratios can be misinterpreted as increases in MetHb levels associated with NO-dependent heme oxidation. Conversely, any decrease in levels of pentacoordinate NO-Hb can be misinterpreted as a disappearance of MetHb associated with NO-dependent heme reduction. Transitions between pentacoordinate and hexacoordinate forms of NO-Hb with spectral changes suggestive of changes in levels of heme-bound NO are sensitive to the protein's quaternary conformation and can be brought about by alterations in anion levels or the degree of heme saturation with either O2 or NO. | lld:pubmed |
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| pubmed-article:14514887 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14514887 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14514887 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14514887 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14514887 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14514887 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:14514887 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:14514887 | pubmed:author | pubmed-author:BimbotLL | lld:pubmed |
| pubmed-article:14514887 | pubmed:author | pubmed-author:PetersonJimJ | lld:pubmed |
| pubmed-article:14514887 | pubmed:author | pubmed-author:PearceLinda... | lld:pubmed |
| pubmed-article:14514887 | pubmed:author | pubmed-author:CrumblissAlvi... | lld:pubmed |
| pubmed-article:14514887 | pubmed:author | pubmed-author:FagoAngelaA | lld:pubmed |
| pubmed-article:14514887 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14514887 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:14514887 | pubmed:volume | 100 | lld:pubmed |
| pubmed-article:14514887 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14514887 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14514887 | pubmed:pagination | 12087-92 | lld:pubmed |
| pubmed-article:14514887 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:meshHeading | pubmed-meshheading:14514887... | lld:pubmed |
| pubmed-article:14514887 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14514887 | pubmed:articleTitle | The case of the missing NO-hemoglobin: spectral changes suggestive of heme redox reactions reflect changes in NO-heme geometry. | lld:pubmed |
| pubmed-article:14514887 | pubmed:affiliation | Nicholas School of the Environment and Earth Sciences, Duke University, Beaufort, NC 28516, USA. | lld:pubmed |
| pubmed-article:14514887 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14514887 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:14514887 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:14514887 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:14514887 | lld:pubmed |
