Structure of Hemoglobin M Boston, a Variant with a Five-Coordinated Ferric Heme

AUTOR(ES)

Pulsinelli, P. D.

RESUMO

X-ray analysis of the natural valency hybrid α2+M Bostonβ2deoxy shows that the ferric iron atoms in the abnormal α subunits are bonded to the phenolate side chains of the tyrosines that have replaced the distal histidines; the iron atoms are displaced to the distal side of the porphyrin ring and are not bonded to the proximal histidines. The resulting changes in tertiary structure of the α subunits stabilize the hemoglobin tetramer in the quaternary deoxy structure, which lowers the oxygen affinity of the normal β subunits and causes cyanosis. The strength of the bond from the ferric iron to the phenolate oxygen appears to be the main factor responsible for the many abnormal properties of hemoglobin M Boston.

Documentos Relacionados

• Functional and physicochemical studies of hemoglobin St. Louis beta 28 (B10) Leu replaced by Gln: a variant with ferric beta heme iron.
• GEORGE STRONG DERBY, of Boston, Mass
• A organização dos imigrantes brasileiros em Boston, EUA
• Mortality in a Movie Projectionist Union in Boston, 1910-64
• THE ANNUAL MEETING. BOSTON, JUNE 6 TO 8, 1921