期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 112, 期 43, 页码 13123-13127出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1515704112
关键词
heme; bioinorganic; magnetism; oxygen transport; metalloproteins
资金
- National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health [R01DK019038]
- National Science Foundation [CHE-1409929]
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1409929] Funding Source: National Science Foundation
Two articles published by Pauling and Coryell in PNAS nearly 80 years ago described in detail the magnetic properties of oxy- and deoxyhemoglobin, as well as those of closely related compounds containing hemes. Their measurements revealed a large difference in magnetism between oxygenated and deoxygenated forms of the protein and, along with consideration of the observed diamagnetism of the carbonmonoxy derivative, led to an electronic structural formulation of oxyhemoglobin. The key role of hemoglobin as the main oxygen carrier in mammalian blood had been established earlier, and its allosteric behavior had been described in the 1920s. The Pauling-Coryell articles on hemoglobin represent truly seminal contributions to the field of bioinorganic chemistry because they are the first to make connections between active site electronic structure and the function of a metalloprotein.
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