Linked Life Data

15154794

Source:http://linkedlifedata.com/resource/pubmed/id/15154794

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2004-5-24
pubmed:abstractText
The isolation and the X-ray crystal structure of physiological copper(II)-L-histidine complex are reported. The neutral five-coordinate complex shows distorted square pyramidal geometry with bidentate and tridentate L-histidine ligands. The basic character of the pendent imidazole group and H-bonding interactions of bidentate L-histidine ligand are important for copper transport. The unique structural features help explain the origin of its thermodynamic stability and kinetic reactivity in human blood along with the ternary copper(II)-amino acid complexes. The role of L-histidine in interaction with copper(II)-albumin, in cellular uptake of copper, and in treatment of Menkes disease can be studied using these results.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0020-1669
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3338-40
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
X-ray structure of physiological copper(II)-bis(L-histidinato) complex.
pubmed:affiliation
Department of Structural Biology and Biochemistry, The Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't