| pubmed-article:7696465 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7696465 | lifeskim:mentions | umls-concept:C0205108 | lld:lifeskim |
| pubmed-article:7696465 | lifeskim:mentions | umls-concept:C0019602 | lld:lifeskim |
| pubmed-article:7696465 | lifeskim:mentions | umls-concept:C0027078 | lld:lifeskim |
| pubmed-article:7696465 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:7696465 | lifeskim:mentions | umls-concept:C0596957 | lld:lifeskim |
| pubmed-article:7696465 | lifeskim:mentions | umls-concept:C0597557 | lld:lifeskim |
| pubmed-article:7696465 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:7696465 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:7696465 | pubmed:dateCreated | 1995-5-3 | lld:pubmed |
| pubmed-article:7696465 | pubmed:abstractText | Four independent 90 ps molecular dynamics simulations of sperm-whale wild-type carbonmonoxy myoglobin (MbCO) have been calculated using a new AMBER force field for the haem prosthetic group. Two trajectories have the distal 64N delta nitrogen protonated, and two have the 64N epsilon nitrogen protonated; all water molecules within 16 A of the carbonyl O are included. In three trajectories, the distal residue remains part of the haem pocket, with the protonated distal nitrogen pointing into the active site. This is in contrast with the neutron diffraction crystal structure, but is consistent with the solution phase CO stretching frequencies (upsilon CO) of MbCO and various of its mutants. There are significant differences in the "closed" pocket structures found for each tautomer: the 64N epsilon H trajectories both show stable distal-CO interactions, whereas the 64N delta H tautomer) has a weaker interaction resulting in a more mobile distal side chain. One trajectory (a 64N delta H tautomer) has the distal histidine moving out into the "solvent", leaving the pocket in an "open" structure, with a large unhindered entrance to the active site. These trajectories suggest that the three upsilon CO frequencies observed for wild-type MbCO in solution, rather than representing significantly different Fe-C-O geometries as such, arise from three different haem pocket structures, each with different electric fields at the ligand. Each pocket structure corresponds to a different distal histidine conformer: the A3 band to the 64N epsilon H tautomer, the A1,2 band to the 64N delta H tautomer, and the A0 band to the absence of any significant interaction with the distal side chain. | lld:pubmed |
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| pubmed-article:7696465 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7696465 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7696465 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7696465 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7696465 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:7696465 | pubmed:author | pubmed-author:KitagawaTT | lld:pubmed |
| pubmed-article:7696465 | pubmed:author | pubmed-author:JewsburyPP | lld:pubmed |
| pubmed-article:7696465 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7696465 | pubmed:volume | 67 | lld:pubmed |
| pubmed-article:7696465 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7696465 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7696465 | pubmed:pagination | 2236-50 | lld:pubmed |
| pubmed-article:7696465 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7696465 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7696465 | pubmed:articleTitle | The distal residue-CO interaction in carbonmonoxy myoglobins: a molecular dynamics study of two distal histidine tautomers. | lld:pubmed |
| pubmed-article:7696465 | pubmed:affiliation | Institute for Molecular Science, Okazaki, Japan. | lld:pubmed |
| pubmed-article:7696465 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7696465 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7696465 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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