Tryptophan residues in native and reoxidized muramidase: Luminescence properties

Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis Pub Date : 1966-07-13 DOI:10.1016/0926-6585(66)90307-4

Jorge E. Churchich

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引用次数: 27

Abstract

The luminiscence properties of tryptophan chromophores in muramidase are affected by changes in enzyme conformation.

Fluorimetric measurements indicated that the emission spectrum of native muramidase (λ_max. = 337 mμ) was shifted toward longer wavelengths (λ_max. = 350 mμ) as a result of structural changes produced by disruption and carboxymethylation of disulfide bonds. When the disulfide bonds were reformed at pH 8, the emission spectra of reoxidized muramidase resemble that of native muramidase with regard to both general structure and band position.

The phosphorescence spectra of the muramidase species revealed the predominant contribution of tryptophan chromophores to the long-lived emission, and this observation was substantiated by decay-time measurements.

The τ_p values of native and reoxidized muramidases (τ_p = 1−1.9 sec) were remarkably shorter than the τ_p value of reduced carboxymethylated muramidase (τ_p = 4.1 sec). The possible significance of these phosphorescence and fluorescence studies are discussed.

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天然和再氧化酶中的色氨酸残基:发光性质

酶构象的改变影响着酶中色氨酸发色团的发光特性。荧光测定表明，天然酶(λmax;= 337 μ m)向更长的波长(λmax。= 350 μ m)，这是由于二硫键的破坏和羧甲基化引起的结构变化。当二硫键在pH 8下重组时，再氧化酶的发射光谱在一般结构和能带位置上与天然酶相似。酶的磷光光谱揭示了色氨酸发色团对长寿命发射的主要贡献，这一观察结果通过衰变时间测量得到证实。原生酶和再氧化酶的τp值(τp = 1 ~ 1.9 sec)明显短于还原羧甲基化酶的τp值(τp = 4.1 sec)。讨论了这些磷光和荧光研究的可能意义。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis

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