Heterogeneity of the isolated subunits of the fetal and adult human hemoglobin in solution, detected by XANES spectroscopy.
Differences in the local structure of the heme in the isolated alpha-, beta- and gamma-chains of the adult and fetal human hemoglobin are detected by XANES (X-ray absorption near-edge structure) spectroscopy. The ligand bonding angle to the iron ion in the ligated forms and the displacement of the Fe respect to the porphyrin plane in the deoxy forms are found to be different for each chain.
Congiu Castellano
A
A
Dipartimento di Fisica, Università La Sapienza, Roma, Italy.
Castagnola
M
M
Burattini
E
E
Dell'Ariccia
M
M
Della Longa
S
S
Giovannelli
A
A
Durham
P J
PJ
Bianconi
A
A
D002248:Carbon Monoxide; D005319:Fetal Hemoglobin / Q000032:analysis* / Q000502:physiology; D006441:Hemoglobin A / Q000032:analysis* / Q000502:physiology; D006801:Humans; D015394:Molecular Structure; D010100:Oxygen; D013057:Spectrum Analysis / Q000379:methods; D013329:Structure-Activity Relationship; D014965:X-Rays
D002248:Carbon Monoxide; D006441:Hemoglobin A; D005319:Fetal Hemoglobin; D010100:Oxygen