{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,29]],"date-time":"2026-07-29T20:51:16Z","timestamp":1785358276350,"version":"3.55.0"},"reference-count":0,"publisher":"National Academy of Sciences","issue":"12","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[1973,12]]},"abstract":"<jats:p>\n                    X-ray analysis of the natural valency hybrid \u03b1\n                    <jats:sub>2<\/jats:sub>\n                    <jats:sup>+M Boston<\/jats:sup>\n                    \u03b2\n                    <jats:sub>2<\/jats:sub>\n                    <jats:sup>deoxy<\/jats:sup>\n                    shows that the ferric iron atoms in the abnormal \u03b1 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 \u03b1 subunits stabilize the hemoglobin tetramer in the quaternary deoxy structure, which lowers the oxygen affinity of the normal \u03b2 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.\n                  <\/jats:p>","DOI":"10.1073\/pnas.70.12.3870","type":"journal-article","created":{"date-parts":[[2006,5,31]],"date-time":"2006-05-31T02:40:38Z","timestamp":1149043238000},"page":"3870-3874","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":65,"title":["Structure of Hemoglobin M Boston, a Variant with a Five-Coordinated Ferric Heme"],"prefix":"10.1073","volume":"70","author":[{"given":"P. D.","family":"Pulsinelli","sequence":"first","affiliation":[{"name":"MRC Laboratory of Molecular Biology, Cambridge, England"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. F.","family":"Perutz","sequence":"additional","affiliation":[{"name":"MRC Laboratory of Molecular Biology, Cambridge, England"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. L.","family":"Nagel","sequence":"additional","affiliation":[{"name":"Department of Medicine, Albert Einstein College of Medicine of Yeshiva University, Bronx, New York, 10461, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[1973,12]]},"container-title":["Proceedings of the National Academy of Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/pnas.org\/doi\/pdf\/10.1073\/pnas.70.12.3870","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,4,13]],"date-time":"2022-04-13T10:47:30Z","timestamp":1649846850000},"score":1,"resource":{"primary":{"URL":"https:\/\/pnas.org\/doi\/full\/10.1073\/pnas.70.12.3870"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[1973,12]]},"references-count":0,"journal-issue":{"issue":"12","published-print":{"date-parts":[[1973,12]]}},"alternative-id":["10.1073\/pnas.70.12.3870"],"URL":"https:\/\/doi.org\/10.1073\/pnas.70.12.3870","relation":{},"ISSN":["0027-8424","1091-6490"],"issn-type":[{"value":"0027-8424","type":"print"},{"value":"1091-6490","type":"electronic"}],"subject":[],"published":{"date-parts":[[1973,12]]},"assertion":[{"value":"1973-12-01","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}