期刊
PHYSICAL REVIEW LETTERS
卷 102, 期 6, 页码 -出版社
AMER PHYSICAL SOC
DOI: 10.1103/PhysRevLett.102.068103
关键词
-
Soft-x-ray absorption spectroscopy at the L(2,3) edge of the iron center in bovine hemoglobin and hemin under physiological conditions is reported for the first time. Spectra of the same compounds in solid form are presented for comparison. Striking differences in the electronic structure of the metalloporphyrin are observed between the liquid and solid compounds. We unambiguously show that hemoglobin and hemin are in a high-spin ferric state in solution, and that the 2p spin-orbit coupling decreases for hemin compared to the hemoglobin, while this is not the case in solids. The spectra were simulated using ligand field multiplet theory, in good agreement with the experiment, allowing quantification of the amount of charge transfer between the porphyrin and Fe(3+) ion in hemoglobin and in hemin.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据