期刊
JOURNAL OF PHYSICAL CHEMISTRY LETTERS
卷 4, 期 18, 页码 3031-3038出版社
AMER CHEMICAL SOC
DOI: 10.1021/jz4016266
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资金
- KAKENHI [23550019]
- Mitsubishi Foundation
- NSF [MCB-1051590]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1051590] Funding Source: National Science Foundation
- Grants-in-Aid for Scientific Research [23550019] Funding Source: KAKEN
Many biological cofactors, such as light-absorbing chromophores in photoreceptors, are intrinsically planar molecules. A protein environment, however, causes structural distortions of the cofactor, and such structural changes can lead to a modulation of chemical properties of the cofactor to maximize its biological activity. Here, we investigate the active site structure of photoactive yellow protein (PYP), a blue light photoreceptor that contains a p-coumaric acid (pCA) chromophore, by a near-infrared excited Raman optical activity (ROA). Specifically, we measured the ROA spectra of PYP, whose chromophore is replaced with a locked pCA analogue. Furthermore, we show that a spectral analysis based on quantum mechanical/molecular mechanical (QM/MM) calculations of the whole protein molecule is useful to obtain structural information from the observed ROA spectra. The use of the near-infrared ROA combined with QM/MM calculations is a novel and generally applicable spectroscopic tool to study the chromophore distortions within a protein environment.
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