Muhoberac B B, Shelnutt J A, Ondrias M R
Department of Chemistry, Purdue University School of Science, Indiana University-Purdue University at Indianapolis 46223.
FEBS Lett. 1988 Feb 15;228(2):310-6. doi: 10.1016/0014-5793(88)80022-x.
The interactions of ethanol and methanol with ferrihemoglobin were examined using resonance Raman spectroscopy. After binding either alcohol, the low-frequency resonance Raman spectra of human ferrihemoglobin are almost identical to the unperturbed spectrum except for shifts in the 309 cm-1 band to higher frequency by as much as 8 cm-1. The ethanol-induced shift is greater than that with methanol even though complex formation was less for ethanol than methanol. The spectral changes imply a site-specific, similar binding of these alcohols to ferrihemoglobin which may involve steric interactions. Possible assignments of the 309 cm-1 band to structural features as well as potential mechanisms of the alcohol-induced spectral changes are discussed.
使用共振拉曼光谱研究了乙醇和甲醇与高铁血红蛋白的相互作用。结合任何一种醇后，人高铁血红蛋白的低频共振拉曼光谱与未受干扰的光谱几乎相同，只是309 cm-1波段的频率向高频移动了多达8 cm-1。尽管乙醇形成的复合物比甲醇少，但乙醇引起的位移大于甲醇引起的位移。光谱变化表明这些醇与高铁血红蛋白存在位点特异性的相似结合，这可能涉及空间相互作用。讨论了将309 cm-1波段归属于结构特征的可能性以及醇诱导光谱变化的潜在机制。
