| pubmed-article:8260499 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8260499 | lifeskim:mentions | umls-concept:C0030065 | lld:lifeskim |
| pubmed-article:8260499 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:8260499 | lifeskim:mentions | umls-concept:C0231881 | lld:lifeskim |
| pubmed-article:8260499 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:8260499 | pubmed:issue | 51 | lld:pubmed |
| pubmed-article:8260499 | pubmed:dateCreated | 1994-1-25 | lld:pubmed |
| pubmed-article:8260499 | pubmed:abstractText | The binding of ferrous and ferric hemes and manganese(II)- and manganese(III)-substituted hemes to heme oxygenase has been investigated by optical absorption, resonance Raman, and EPR spectroscopy. The results are consistent with the presence of a six-coordinate heme moiety ligated to an essential histidine ligand and a water molecule. The latter ionizes with a pKa approximately 8.0 to give a mixture of high-spin and low-spin six-coordinate hydroxo adducts. Addition of excess cyanide converts the heme to a hexacoordinate low-spin species. The resonance Raman spectrum of the ferrous heme-heme oxygenase complex and that of the Mn(II)protoporphyrin-heme oxygenase complex shows bands at 216 and 212 cm-1, respectively, that are assigned to the metal-histidine stretching mode. The EPR spectrum of the oxidized heme-heme oxygenase complex has a strongly axial signal with g parallel of approximately 6 and g perpendicular approximately 2. 14NO and 15NO adducts of ferrous heme-heme oxygenase exhibit EPR hyperfine splittings of approximately 20 and approximately 25 Gauss, respectively. In addition, both nitrosyl complexes show additional superhyperfine splittings of approximately 7 Gauss from spin-spin interaction with the proximal histidine nitrogen. The heme environment in the heme-heme oxygenase enzyme-substrate complex has spectroscopic properties similar to those of the heme in myoglobin. Hence, there is neither a strongly electron-donating fifth (proximal) ligand nor an electron-withdrawing network on the distal side of the heme moiety comparable to that for cytochromes P-450 and peroxidases. This observation has profound implications about the nature of the oxygen-activating process in the heme-->biliverdin reaction that are discussed in this paper. | lld:pubmed |
| pubmed-article:8260499 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8260499 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8260499 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8260499 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8260499 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8260499 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8260499 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8260499 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8260499 | pubmed:author | pubmed-author:Ortiz de... | lld:pubmed |
| pubmed-article:8260499 | pubmed:author | pubmed-author:LoehrT MTM | lld:pubmed |
| pubmed-article:8260499 | pubmed:author | pubmed-author:SunJJ | lld:pubmed |
| pubmed-article:8260499 | pubmed:author | pubmed-author:WillePP | lld:pubmed |
| pubmed-article:8260499 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8260499 | pubmed:day | 28 | lld:pubmed |
| pubmed-article:8260499 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8260499 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8260499 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8260499 | pubmed:pagination | 14151-7 | lld:pubmed |
| pubmed-article:8260499 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8260499 | pubmed:meshHeading | pubmed-meshheading:8260499-... | lld:pubmed |
| pubmed-article:8260499 | pubmed:meshHeading | pubmed-meshheading:8260499-... | lld:pubmed |
| pubmed-article:8260499 | pubmed:meshHeading | pubmed-meshheading:8260499-... | lld:pubmed |
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| pubmed-article:8260499 | pubmed:meshHeading | pubmed-meshheading:8260499-... | lld:pubmed |
| pubmed-article:8260499 | pubmed:meshHeading | pubmed-meshheading:8260499-... | lld:pubmed |
| pubmed-article:8260499 | pubmed:meshHeading | pubmed-meshheading:8260499-... | lld:pubmed |
| pubmed-article:8260499 | pubmed:meshHeading | pubmed-meshheading:8260499-... | lld:pubmed |
| pubmed-article:8260499 | pubmed:meshHeading | pubmed-meshheading:8260499-... | lld:pubmed |
| pubmed-article:8260499 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8260499 | pubmed:articleTitle | Resonance Raman and EPR spectroscopic studies on heme-heme oxygenase complexes. | lld:pubmed |
| pubmed-article:8260499 | pubmed:affiliation | Department of Chemistry, Biochemistry, and Molecular Biology, Oregon Graduate Institute of Science and Technology, Portland 97291-1000. | lld:pubmed |
| pubmed-article:8260499 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8260499 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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