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

P. D. Pulsinelli | Zendy; M. F. Perutz | Zendy; R L Nagel | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

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

Author(s) -

P. D. Pulsinelli,

M. F. Perutz,

R L Nagel

Publication year - 1973

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.70.12.3870

Subject(s) - tetramer , ferric , heme , chemistry , protein quaternary structure , hemoglobin , valency , hemeprotein , porphyrin , crystallography , side chain , oxygen , stereochemistry , protein subunit , biochemistry , inorganic chemistry , enzyme , organic chemistry , linguistics , philosophy , gene , polymer

X-ray analysis of the natural valency hybrid α2 +M Boston β2 deoxy 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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research