期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1973
卷号：70
期号：12
页码：3870-3874
DOI：10.1073/pnas.70.12.3870
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：X-ray analysis of the natural valency hybrid [α]2+M Boston{beta}2deoxy 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 {beta} 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.
