Source:http://linkedlifedata.com/resource/pubmed/id/15844231
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
11-12
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pubmed:dateCreated |
2005-4-20
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pubmed:abstractText |
Hemoglobin and related heme proteins, generally referred to as 'globins', reversibly bind gaseous diatomic ligands (O2, NO, and CO) to a penta-coordinate heme iron atom, the ligand filling the sixth coordination site. Over the last decade, several new globins have been reported to display a functionally-relevant hexa-coordinate heme iron atom, whose sixth coordination site is taken by an endogenous protein ligand. The reversible intramolecular hexa- to penta-coordination process at the heme-Fe atom modulates exogenous ligand binding properties of hexa-coordinate globins. Here, we review current knowledge on hexa-coordinate globins in terms of their structural and functional properties.
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pubmed:commentsCorrections | |
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:issn |
1521-6543
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
56
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
643-51
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15844231-Animals,
pubmed-meshheading:15844231-Heme,
pubmed-meshheading:15844231-Hemoglobins,
pubmed-meshheading:15844231-Humans,
pubmed-meshheading:15844231-Ligands,
pubmed-meshheading:15844231-Protein Binding,
pubmed-meshheading:15844231-Protein Structure, Tertiary,
pubmed-meshheading:15844231-Structure-Activity Relationship,
pubmed-meshheading:15844231-Synechocystis
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pubmed:articleTitle |
Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family.
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pubmed:affiliation |
Department of Physics-INFM, Center for Excellence in Biomedical Research, University of Genova, Via Dodecaneso 33, I-16146 Genova, Italy.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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