RESONANCE RAMAN STUDIES OF MYOGLOBIN SINGLE-CRYSTALS
RESONANCE RAMAN STUDIES OF MYOGLOBIN SINGLE-CRYSTALS
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DOI：
10.1021/ja00227a011
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发表时间：
1988-09-14
影响因子：
15
通讯作者：
CHAMPION, PM
中科院分区：
文献类型：
--
作者：
MORIKIS, D;SAGE, JT;CHAMPION, PM
We investigate the resonance Raman scattering of myoglobin (Mb) single crystals in order to probe the similarities and/or differences between solution and crystal structures of biological molecules. Resonant light scattering spectroscopy provides a high-resolution map of the vibrational frequencies associated with the protein active site and can be applied to solution, crystalline, or frozen states of the sample. We find that the metmyoglobin samples have active site heme structures that are nearly independent of the sample state. However, when the carbon monoxide adduct is formed, the MbCO crystal spectrum reveals two distinct modes of CO binding, compared to a single Raman mode in the solution structure. Unusual observations involving the photoreduction of metMb and the photolysis of MbCO in the crystalline state are also reported. A preliminary polarization analysis of the Raman scattering from Mb crystals is also presented.
