Discovery of the magnetic behavior of hemoglobin: A beginning of bioinorganic chemistry.
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.
Department of Chemistry, University of Rochester, Rochester, NY 14627;
Kara L
KL
Bren
Department of Chemistry, University of Rochester, Rochester, NY 14627; eisenberg@chem.rochester.edu.
Richard
R
Eisenberg
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125; Beckman Institute, California Institute of Technology, Pasadena, CA 91125.
Harry B
HB
Gray
D000818:Animals; D006454:Hemoglobins / Q000737:chemistry*; D007287:Inorganic Chemicals / Q000737:chemistry; D008280:Magnetics
D006454:Hemoglobins; D007287:Inorganic Chemicals
bioinorganic; heme; magnetism; metalloproteins; oxygen transport