| pubmed-article:6253470 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6253470 | lifeskim:mentions | umls-concept:C0026336 | lld:lifeskim |
| pubmed-article:6253470 | lifeskim:mentions | umls-concept:C0013846 | lld:lifeskim |
| pubmed-article:6253470 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:6253470 | lifeskim:mentions | umls-concept:C0010796 | lld:lifeskim |
| pubmed-article:6253470 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:6253470 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:6253470 | pubmed:dateCreated | 1981-1-29 | lld:pubmed |
| pubmed-article:6253470 | pubmed:abstractText | A hypothetical three-dimensional model of the cytochrome c peroxidase . tuna cytochrome c complex is presented. The model is based on known x-ray structures and supported by chemical modification and kinetic data. Cytochrome c peroxidase contains a ring of aspartate residues with a spatial distribution on the molecular surface that is complementary to the distribution of highly conserved lysines surrounding the exposed edge of the cytochrome c heme crevice, namely lysines 13, 27, 72, 86, and 87. These lysines are known to play a functional role in the reaction with cytochrome c peroxidase, cytochrome oxidase, cytochrome c1, and cytochrome b5. A hypothetical model of the complex was constructed with the aid of a computer-graphics display system by visually optimizing hydrogen bonding interactions between complementary charged groups. The two hemes in the resulting model are parallel with an edge separation of 16.5 A. In addition, a system of inter- and intramolecular pi-pi and hydrogen bonding interactions forms a bridge between the hemes and suggests a mechanism of electron transfer. | lld:pubmed |
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| pubmed-article:6253470 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6253470 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6253470 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6253470 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:6253470 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6253470 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:6253470 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:6253470 | pubmed:author | pubmed-author:KrautJJ | lld:pubmed |
| pubmed-article:6253470 | pubmed:author | pubmed-author:PoulosT LTL | lld:pubmed |
| pubmed-article:6253470 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6253470 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:6253470 | pubmed:volume | 255 | lld:pubmed |
| pubmed-article:6253470 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6253470 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6253470 | pubmed:pagination | 10322-30 | lld:pubmed |
| pubmed-article:6253470 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:6253470 | pubmed:year | 1980 | lld:pubmed |
| pubmed-article:6253470 | pubmed:articleTitle | A hypothetical model of the cytochrome c peroxidase . cytochrome c electron transfer complex. | lld:pubmed |
| pubmed-article:6253470 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6253470 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6253470 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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