Bren Kara L, Eisenberg Richard, Gray Harry B
Department of Chemistry, University of Rochester, Rochester, NY 14627;
Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, CA 91125; Beckman Institute, California Institute of Technology, Pasadena, CA 91125.
Proc Natl Acad Sci U S A. 2015 Oct 27;112(43):13123-7. doi: 10.1073/pnas.1515704112.
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.
近80年前,鲍林(Pauling)和科里尔(Coryell)在《美国国家科学院院刊》(PNAS)上发表的两篇文章详细描述了氧合血红蛋白和脱氧血红蛋白以及含血红素的密切相关化合物的磁性。他们的测量揭示了该蛋白质氧化态和脱氧态之间的磁性存在巨大差异,并且结合对观察到的碳氧血红蛋白衍生物抗磁性的考虑,得出了氧合血红蛋白的电子结构公式。血红蛋白作为哺乳动物血液中主要氧载体的关键作用早在之前就已确立,其变构行为在20世纪20年代就已被描述。鲍林 - 科里尔关于血红蛋白的文章对生物无机化学领域做出了真正具有开创性的贡献,因为它们首次建立了活性位点电子结构与金属蛋白功能之间的联系。