Source:http://linkedlifedata.com/resource/pubmed/id/21204537
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
2011-2-3
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pubmed:abstractText |
CORM-3, [fac-Ru(CO)(3)Cl(?(2)-H(2)NCH(2)CO(2))], is a well-known carbon monoxide releasing molecule (CORM) capable of delivering CO in vivo. Herein we show for the first time that the interactions of CORM-3 with proteins result in the loss of a chloride ion, glycinate, and one CO ligand. The rapid formation of stable adducts between the protein and the remaining cis-Ru(II)(CO)(2) fragments was confirmed by Inductively Coupled Plasma-Atomic Emission Spectroscopy (ICP-AES), Liquid-Chromatography Mass Spectrometry (LC-MS), Infrared Spectroscopy (IR), and X-ray crystallography. Three Ru coordination sites are observed in the structure of hen egg white lysozyme crystals soaked with CORM-3. The site with highest Ru occupancy (80%) shows a fac-[(His15)Ru(CO)(2)(H(2)O)(3)] structure.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1520-5126
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
9
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pubmed:volume |
133
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1192-5
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pubmed:meshHeading |
pubmed-meshheading:21204537-Animals,
pubmed-meshheading:21204537-Blood Proteins,
pubmed-meshheading:21204537-Crystallography, X-Ray,
pubmed-meshheading:21204537-Models, Molecular,
pubmed-meshheading:21204537-Muramidase,
pubmed-meshheading:21204537-Organometallic Compounds,
pubmed-meshheading:21204537-Protein Binding,
pubmed-meshheading:21204537-Protein Conformation
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pubmed:year |
2011
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pubmed:articleTitle |
CORM-3 reactivity toward proteins: the crystal structure of a Ru(II) dicarbonyl-lysozyme complex.
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pubmed:affiliation |
REQUIMTE-CQFB, Departamento de Qui?mica, FCT-UNL, 2829-516 Caparica, Portugal.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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