Linked Life Data

21491555

Source:http://linkedlifedata.com/resource/pubmed/id/21491555

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2011-5-27
pubmed:abstractText
Spectroscopic and crystallographic evidence of endogenous (His) ligation at the sixth coordination site of the heme iron has been reported for monomeric, dimeric, and tetrameric hemoglobins (Hbs) in both ferrous (hemochrome) and ferric (hemichrome) oxidation states. In particular, the ferric bis- histidyl adduct represents a common accessible ordered state for the ? chains of all tetrameric Hbs isolated from Antarctic and sub-Antarctic fish. Indeed, the crystal structures of known tetrameric Hbs in the bis-His state are characterized by a different binding state of the ? and ? chains. An overall analysis of the bis-histidyl adduct of globin structures deposited in the Protein Data Bank reveals a marked difference between hemichromes in tetrameric Hbs compared to monomeric/dimeric Hbs. Herein, we review the structural, spectroscopic and stability features of hemichromes in tetrameric Antarctic fish Hbs. The role of bis-histidyl adducts is also addressed in a more evolutionary context alongside the concept of its potential physiological role.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1521-6551
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Wiley Periodicals, Inc.
pubmed:issnType
Electronic
pubmed:volume
63
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
295-303
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Occurrence and formation of endogenous histidine hexa-coordination in cold-adapted hemoglobins.
pubmed:affiliation
Department of Chemistry "Paolo Corradini," University of Naples "Federico II," Complesso Universitario Monte S. Angelo, Italy.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't