Boso B, Debrunner P G, Wagner G C, Inubushi T
Biochim Biophys Acta. 1984 Dec 7;791(2):244-51. doi: 10.1016/0167-4838(84)90015-3.
We measured Mössbauer spectra of human oxyhemoglobin, its isolated beta chains, and of oxymyoglobin from horse and sperm whale in fields of 4 or 6 T between 4.2 and 200 K in order to characterize the electronic state of the oxyheme complex. Diamagnetic sodium nitroprusside measured under the same conditions served as a control. The spectra of all compounds are reproduced adequately by a model that assumes a diagmagnetic iron and treats the quadrupole splitting, the asymmetry parameter and the Mössbauer linewidth as adjustable parameters. The results provide no indication in the oxyhemeproteins of the excited triplet state that was postulated by Cerdonio and co-workers (Cerdonio, M., Congiu-Castellano, A., Mogno, F., Pispisa, B., Romani, G.L. and Vitale, S. (1977) Proc. Natl. Acad. Sci. USA 74, 398-400) on the basis of susceptibility measurements on oxyhemoglobin.
我们测量了人氧合血红蛋白、其分离的β链以及马和抹香鲸的氧合肌红蛋白在4.2至200 K温度范围内4 T或6 T磁场中的穆斯堡尔谱，以表征氧合血红素复合物的电子态。在相同条件下测量的抗磁性硝普钠用作对照。所有化合物的谱图都可以通过一个模型充分再现，该模型假设铁为抗磁性，并将四极分裂、不对称参数和穆斯堡尔线宽作为可调参数。结果并未表明氧合血红蛋白蛋白中存在Cerdonio及其同事（Cerdonio, M., Congiu-Castellano, A., Mogno, F., Pispisa, B., Romani, G.L. 和 Vitale, S. (1977) Proc. Natl. Acad. Sci. USA 74, 398 - 400）基于对氧合血红蛋白的磁化率测量所假设的激发三重态。
