Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11-12
pubmed:dateCreated
2005-4-20
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.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1521-6543
pubmed:author
pubmed:issnType
Print
pubmed:volume
56
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
643-51
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
Structure-function relationships in the growing hexa-coordinate hemoglobin sub-family.
pubmed:affiliation
Department of Physics-INFM, Center for Excellence in Biomedical Research, University of Genova, Via Dodecaneso 33, I-16146 Genova, Italy.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't