IRON SITE STRUCTURE OF 2 IRREVERSIBLE HEMICHROMES FROM HUMAN HEMOGLOBIN, UNTREATED AND OXIDIZED TO SULFOXIDE AT METD6(55)BETA

Authors
DELLALONGA S AMICONI G SALAH OA ASCONE I BARTERI M BERTOLLINI A BIANCONI A CASTELLANO AC
Citation
S. Dellalonga et al., IRON SITE STRUCTURE OF 2 IRREVERSIBLE HEMICHROMES FROM HUMAN HEMOGLOBIN, UNTREATED AND OXIDIZED TO SULFOXIDE AT METD6(55)BETA, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1294(1), 1996, pp. 72-76
Citations number
27
Categorie Soggetti
Biology,Biophysics
Journal title
Biochimica et biophysica acta. Protein structure and molecular enzymology → ACNP
ISSN journal
01674838
Volume
1294
Issue
1
Year of publication
1996
Pages
72 - 76
Database
ISI
SICI code
0167-4838(1996)1294:1<72:ISSO2I>2.0.ZU;2-W
Abstract
The Fe K-edge X-ray absorption near-edge structure (XANES) spectra of two irreversible human hemichromes, spontaneously formed from HbA and HbMetSO (a hemoglobin derivative, where MetD6(55)beta has been previou sly oxidized to sulfoxide by chloramine T) were determined. The result s show that the hemichrome from HbMetSO is characterized by the distal histidyl imidazole moved within the bonding distance of the heme iron . Such structure is different from that of the hemichrome spontaneousl y produced from native human hemoglobin, which probably has a hydroxid e group as sixth heme ligand.