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首页> 外文期刊>Biochemistry >Tyrosine Raman Signatures of the Filamentous Virus Ff Are Diagnostic of Non-Hydrogen-Bonded Phenoxyls:Demonstration by Raman and Infrared Spectroscopy of p-Cresol Vapor
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Tyrosine Raman Signatures of the Filamentous Virus Ff Are Diagnostic of Non-Hydrogen-Bonded Phenoxyls:Demonstration by Raman and Infrared Spectroscopy of p-Cresol Vapor

机译:丝状病毒FF的酪氨酸拉曼签名是非氢键苯氧基的诊断:通过拉曼和磷酸蒸气的拉曼和红外光谱的演示

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摘要

p-Cresol is a simple molecular model for the para phenolic side chain of tyrosine. Previously, Siamwiza and co-workers [(1975) Biochemistry 14, 4870—4876] investigated p-cresol solutions to identify Raman spectroscopic signatures for different hydrogen-bonding states of the tyrosine phenoxyl group in proteins. They found that the phenolic moiety exhibits an intense Raman doublet in the spectral interval 820—860 cm’ and that the doublet intensity ratio (12/h, where 12 and 1~ are Raman peak intensities of the higher- and lower-wavenumber members of the doublet) is diagnostic of specific donor and acceptor roles of the phenoxyl OH group. The range of the doublet intensity ratio in proteins (0.30 <12/il < 2.5) was shown to be governed by Fermi coupling between the phenolic ring-stretching fundamental v1 and the first overtone of the phenolic ring-deformation mode Vi6a, such that when the tyrosine phenoxyl proton is a strong hydrogen-bond donor, 12/11 = 0.30, and when the tyrosine phenoxyl oxygen is a strong hydrogen-bond acceptor, 12/Il = 2.5. Here, we interpret the Raman and infrared spectra of p-cresol vapor and extend the previous correlation to the non-hydrogen-bonded state of the tyrosine phenoxyl group. In the absence of hydrogen bonding, the Raman intensity of the higher-wavenumber component of the canonical Fermi doublet is greatly enhanced such that ‘2/Il = 6.7. Thus, for the non-hydrogen-bonded phenoxyl, the lower-wavenumber member of the Fermi doublet loses most of its Raman intensity. This finding provides a basis for understanding the anomalous Raman singlet signature (—854 cm’) observed for tyrosine in coat protein subunits of filamentous viruses Ff and Pf 1 [Overman, S. A., et al. (1994) Biochemistry 33, 1037—1042; Wen, Z. Q., et al. (1999) Biochemistry 38, 3148—3156]. The implications of the present results for Raman analysis of tyrosine hydrogen-bonding states in other proteins are considered.
机译:p-甲酚是酪氨酸的酚醛侧链的简单分子模型。以前,暹罗和同事[(1975)生物化学14,4870-4876]研究了对甲酚溶液,以鉴定蛋白质中酪氨酸苯氧基的不同氢键状态的拉曼光谱签名。他们发现酚类部分在光谱间隔820-860cm'中表现出强烈的拉曼双峰,并且双层强度比(12 / h,其中12和1〜是高波数构件的拉曼峰值强度双峰)是诺苯氧基OH基团的特定供体和受体作用的诊断。蛋白质中的双重强度比(0.30 <12 / IL <2.5)的范围显示通过FERMI耦合来控制酚类环拉伸基本V1和酚类环形变形模式VI6a的第一个泛孔,使得当酪氨酸苯氧基质子是强氢键供体,12/11 = 0.30,并且当酪氨酸苯氧基氧是强氢粘合受体时,12 / IL = 2.5。这里,我们解释p-cresol蒸气的拉曼和红外光谱,并延伸到与酪氨酸苯氧基的非氢键态的相关性。在不存在氢键的情况下,规范费米双胞胎的高波纹组分的拉曼强度大大增强,使得'2 / IL = 6.7。因此,对于非氢键合的苯氧基,费米双波数构件使其大部分拉曼强度失去。该发现为了解丝状病毒FF和PF1的外套蛋白亚基中观察到对酪氨酸的异常拉曼单次签名(-854cm')提供了基础[Overman,S. A.等人。 (1994)生物化学33,1037-1042; Wen,Z. Q.,等人。 (1999)Biochemistry 38,3148-3156]。考虑了对其他蛋白质中酪氨酸氢键状态的拉曼分析结果的影响。

著录项

  • 来源
    《Biochemistry》 |2001年第8期|共8页
  • 作者单位

    Department of Chemistry Texas A&

    M University College Station Texas 77843-3255 and School of Biological Sciences University of Missouri-Kansas City Kansas City Missouri 64110-2499;

    Department of Chemistry Texas A&

    M University College Station Texas 77843-3255 and School of Biological Sciences University of Missouri-Kansas City Kansas City Missouri 64110-2499;

    Department of Chemistry Texas A&

    M University College Station Texas 77843-3255 and School of Biological Sciences University of Missouri-Kansas City Kansas City Missouri 64110-2499;

    Department of Chemistry Texas A&

    M University College Station Texas 77843-3255 and School of Biological Sciences University of Missouri-Kansas City Kansas City Missouri 64110-2499;

    Department of Chemistry Texas A&

    M University College Station Texas 77843-3255 and School of Biological Sciences University of Missouri-Kansas City Kansas City Missouri 64110-2499;

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  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类 生物化学;
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