| pubmed-article:167834 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C0019944 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C0004492 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C0014406 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C1704241 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C0018966 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C0020923 | lld:lifeskim |
| pubmed-article:167834 | lifeskim:mentions | umls-concept:C2346593 | lld:lifeskim |
| pubmed-article:167834 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:167834 | pubmed:dateCreated | 1975-10-28 | lld:pubmed |
| pubmed-article:167834 | pubmed:abstractText | Horse heart ferric cytochrome c was investigated by the following three methods: (I) Light absorption spectrophotometry at 23 degrees C and 77 degrees K; (II) Electron paramagnetic resonance (EPR) spectroscopy at 20 degrees K; (III) Precise equilibrium measurements of ferric cytochrome c with azide and imidazole between 14.43 and 30.90 degrees C. I and II have demonstrated that: (1) Ferric cytochrome c azide and imidazole complexes were in the purely low spin state between 20 degrees K and 23 degrees C; (2) The energy for the three t2g orbitals calculated in one hole formalism shows that azide or imidazole bind to the heme iron in a similar manner to met-hemoglobin azide or imidazole complexes, respectively. III has demonstrated that: (1) The change of standard enthalpy and that of standard entropy were -2.3 kcal/mol and -1.6 cal/mol per degree for the azide complex formation, and -1.4 kcal/mol and 2.9 cal/mol per degree for the imidazole complex formation. (2) A linear relationship between the change of entropy and that of enthalpy was observed for the above data for the cyanide complex formation. The complex formation of ferric cytochrome c was discussed based on the results of X-ray crystallographic studies compared with hemoglobin and myoglobin. | lld:pubmed |
| pubmed-article:167834 | pubmed:language | eng | lld:pubmed |
| pubmed-article:167834 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:167834 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:167834 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:167834 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:167834 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:167834 | pubmed:author | pubmed-author:IizukaTT | lld:pubmed |
| pubmed-article:167834 | pubmed:author | pubmed-author:Ikeda-SaitoMM | lld:pubmed |
| pubmed-article:167834 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:167834 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:167834 | pubmed:volume | 393 | lld:pubmed |
| pubmed-article:167834 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:167834 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:167834 | pubmed:pagination | 335-42 | lld:pubmed |
| pubmed-article:167834 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:167834 | pubmed:year | 1975 | lld:pubmed |
| pubmed-article:167834 | pubmed:articleTitle | Studies on the heme environment of horse heart ferric cytochrome c. Azide and imidazole complexes of ferric cytochrome c. | lld:pubmed |
| pubmed-article:167834 | pubmed:publicationType | Journal Article | lld:pubmed |
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