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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
14
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pubmed:dateCreated |
1987-6-19
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pubmed:abstractText |
Incorporation of the three synthetic hemins, Fe(III) meso-tetraalkylporphyrins with the methyl, ethyl, or n-propyl groups, into apomyoglobin was followed by spectrophotometry, and the stoichiometric complex formation was confirmed. The reconstituted myoglobins bind with an equimolar amount of cyanide to exhibit visible absorption peaks at 419, 570, and 608 nm. The spectral feature was independent of the cyanide concentrations. Proton NMR spectra of the cyanide complexes resolved the pyrrole-proton signals of the hemins in a -5 to -15-ppm region, which is comparable with that of the corresponding signals of deuterohemin-containing low-spin methemoproteins. These spectral observations indicate the presence of the NC-Fe-N(His-F8) structure in the presently reconstituted cyanide metmyoglobins. The pyrrole-proton NMR signals of the hemins in cyanide metmyoglobins appeared as a singlet, doublet, or quartet for the methyl, ethyl, or n-propyl hemin complexes, respectively. The systematic NMR spectral changes suggest the dynamic free rotation of the alkylhemins about the Fe-N(His-F8) bond. Temperature-dependent NMR spectral transition of the meso-tetraethylhemin-reconstituted myoglobin was consistent with thermally regulated dynamic free rotation of the hemin in the myoglobin heme pocket.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Apoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Hemeproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Mesoporphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/Metmyoglobin,
http://linkedlifedata.com/resource/pubmed/chemical/Myoglobin,
http://linkedlifedata.com/resource/pubmed/chemical/Porphyrins,
http://linkedlifedata.com/resource/pubmed/chemical/apomyoglobin,
http://linkedlifedata.com/resource/pubmed/chemical/cyanometmyoglobin
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
262
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6725-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3571283-Apoproteins,
pubmed-meshheading:3571283-Binding Sites,
pubmed-meshheading:3571283-Heme,
pubmed-meshheading:3571283-Hemeproteins,
pubmed-meshheading:3571283-Magnetic Resonance Spectroscopy,
pubmed-meshheading:3571283-Mesoporphyrins,
pubmed-meshheading:3571283-Metmyoglobin,
pubmed-meshheading:3571283-Myoglobin,
pubmed-meshheading:3571283-Porphyrins,
pubmed-meshheading:3571283-Protein Binding,
pubmed-meshheading:3571283-Spectrophotometry,
pubmed-meshheading:3571283-Thermodynamics
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pubmed:year |
1987
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pubmed:articleTitle |
Proton NMR study of the cyanide metmyoglobin reconstituted with meso-tetraalkylhemins. Dynamic free rotation of the synthetic hemins in the heme pocket.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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