Vibrational Energy Transfer from Heme through Atomic Contacts in Proteins
Vibrational Energy Transfer from Heme through Atomic Contacts in Proteins
复制标题
通过蛋白质中的原子接触从血红素进行振动能量转移
DOI：
10.1021/acs.jpcb.8b03518
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发表时间：
2018
期刊：
影响因子：
--
通讯作者：
Mizutani Yasuhisa
中科院分区：
文献类型：
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作者：
Yamashita Satoshi;Mizuno Misao;Tran Duy Phuoc;Dokainish Hisham;Kitao Akio;Mizutani Yasuhisa
利用时间分辨反斯托克斯紫外共振拉曼光谱结合定点突变技术研究了肌红蛋白的振动能流途径。我们以前的研究表明，蛋白质中的原子接触提供了能量转移的主要途径，而共价键则没有。在本研究中，我们直接检查的贡献的共价键和原子接触的振动能量流的途径，通过比较反斯托克斯共振拉曼光谱的两个肌红蛋白突变体：一个缺乏血红素和多肽链之间的共价键，和其他保留完整的键。这两个突变体的色氨酸带的反斯托克斯拉曼强度的时间变化没有显着差异，这意味着振动能量转移的主导渠道是不是通过共价键，而是通过血红素和蛋白质部分之间的货车范德华原子接触。所获得的见解有助于我们在凝聚相的能量转移的一般理解。
A pathway of vibrational energy flow in myoglobin was studied by time-resolved anti-Stokes ultraviolet resonance Raman spectroscopy combined with site-directed mutagenesis. Our previous study suggested that atomic contacts in proteins provide the dominant pathway for energy transfer while covalent bonds do not. In the present study, we directly examined the contributions of covalent bonds and atomic contacts to the pathway of vibrational energy flow by comparing the anti-Stokes resonance Raman spectra of two myoglobin mutants: one lacked a covalent bond between heme and the polypeptide chain, and the other retained the intact bond. The two mutants showed no significant difference in temporal changes in the anti-Stokes Raman intensities of the tryptophan bands, implying that the dominant channel of vibrational energy transfer is not through the covalent bond but rather through van der Waals atomic contacts between heme and the protein moiety. The obtained insights contribute to our general understanding of energy transfer in the condensed phase.