Structure of the retinal chromophore in the hRL intermediate of halorhodopsin from resonance raman spectroscopy.
Structure of the retinal chromophore in the hRL intermediate of halorhodopsin from resonance raman spectroscopy.
复制标题
共振拉曼光谱中盐视紫红质 hRL 中间体中视网膜发色团的结构。
DOI：
10.1021/bi00395a029
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发表时间：
1987
期刊：
影响因子：
2.9
通讯作者：
Mathies,RA
中科院分区：
文献类型：
--
作者：
Fodor,SP;Bogomolni,RA;Mathies,RA
加州大学伯克利分校化学系Stephen P.A.Fodor，8和Richard A.Mathies*·1加州大学伯克利分校心血管研究所，加州94720，加利福尼亚94143；修订稿件1987年6月12日收到摘要：已获得卤视紫质的HRL中间体的时间分辨共振拉曼光谱。HRL光谱的结构敏感指纹区与细菌视紫红质的L550中间体非常相似，后者具有13-顺式构型。这表明HRL含有一个13-顺式发色团，并且在卤视紫质的光循环中发生了一个全反式的13-顺式异构化。HRL在1644 cm~(-1)处出现Schiff碱伸缩模式，在D20处位移到1620 cm~(-1)，这表明蛋白质上的Schiff碱键是质子化的。CC伸缩模式频率对N-氚的不敏感性表明Schiff碱构型是反的。D20中希夫碱模式的24 cm“1位移表明HRL中的Schiff碱质子与蛋白质有更强的氢键相互作用。
Stephen P. A. Fodor,* 1* Roberto A. Bogomolni, 8 and Richard A. Mathies*· 1 Department of Chemistry, University of California, Berkeley, California 94720, and Cardiovascular Research Institute, University of California, San Francisco, California 94143 Received March 30, 1987; Revised Manuscript Received June 12, 1987 abstract: Time-resolved resonance Raman spectra of the hRL intermediate of halorhodopsin have been obtained. The structurally sensitive fingerprint region of the hRL spectrum is very similar to that of bacteriorhodopsin’s L550 intermediate, which is known to have a 13-cis configuration. This indicates that hRL contains a 13-cis chromophore and that an all-trans 13-cis isomerization occurs in the halorhodopsin photocycle. hRL exhibits a Schiff base stretching modeat 1644 cm-1, which shifts to 1620 cm" 1 in D20. This demonstrates that the Schiff base linkage to the protein is protonated. The insensitivity of the CC stretching mode frequencies to N-deuteriation suggests that the Schiff base configuration is anti. The 24 cm" 1 shift of the Schiff base mode in D20 indicates that the Schiff base proton in hRL has a stronger hydrogen-bonding interaction with the protein than does hR57g.