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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
2003-10-15
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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.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-10430889,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-10455144,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-11300758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-11573011,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-12032284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-12032357,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-12177417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-12468537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-1262343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-171411,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-184818,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-188812,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-209042,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-2827174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-40990,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-4350065,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-4351737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-681362,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-7276933,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-8512319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-8679521,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-9428761,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-9685383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/14514887-9741577
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
100
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12087-92
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14514887-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:14514887-Heme,
pubmed-meshheading:14514887-Hemoglobin A, Glycosylated,
pubmed-meshheading:14514887-Hemoglobins,
pubmed-meshheading:14514887-Humans,
pubmed-meshheading:14514887-Kinetics,
pubmed-meshheading:14514887-Methemoglobin,
pubmed-meshheading:14514887-Nitric Oxide,
pubmed-meshheading:14514887-Oxidation-Reduction,
pubmed-meshheading:14514887-Spectrophotometry
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pubmed:year |
2003
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pubmed:articleTitle |
The case of the missing NO-hemoglobin: spectral changes suggestive of heme redox reactions reflect changes in NO-heme geometry.
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pubmed:affiliation |
Nicholas School of the Environment and Earth Sciences, Duke University, Beaufort, NC 28516, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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