用超快x射线散射揭示环二硫化物中UVC键断裂的反应路径。

IF 11.7 1区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES
Lingyu Ma, Wenpeng Du, Haiwang Yong, Brian Stankus, Jennifer M. Ruddock, Andrés Moreno Carrascosa, Nathan Goff, Yu Chang, Nikola Zotev, Darren Bellshaw, Thomas J. Lane, Mengning Liang, Sébastien Boutet, Sergio Carbajo, Joseph S. Robinson, Jason E. Koglin, Michael P. Minitti, Adam Kirrander, Theis I. Sølling, Peter M. Weber
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引用次数: 0

摘要

二硫键是普遍存在的分子基序,影响着许多蛋白质的三级结构和生物学功能。然而,众所周知,当暴露于紫外线C (UVC)辐射时,二硫键具有光稳定性。深紫外诱导的S─S键在非常快的时间尺度上的断裂动力学对于充分了解蛋白质的光稳定性和光损伤修复机制至关重要。1,2-二thiane是最小的饱和环分子,具有S─S键,模拟生物活性物质,我们利用x射线自由电子激光在200 nm激发下用飞秒时间分辨x射线散射研究了光化学。在飞秒时域,我们发现了一个非常快的反应,它产生一个和两个硫原子的分子碎片。在皮秒和纳秒的时间尺度上,一个复杂的反应网络展开,最终完成硫与母体分子的分离。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Revealing the reaction path of UVC bond rupture in cyclic disulfides with ultrafast x-ray scattering

Revealing the reaction path of UVC bond rupture in cyclic disulfides with ultrafast x-ray scattering
Disulfide bonds are ubiquitous molecular motifs that influence the tertiary structure and biological functions of many proteins. Yet, it is well known that the disulfide bond is photolabile when exposed to ultraviolet C (UVC) radiation. The deep-UV–induced S─S bond fragmentation kinetics on very fast timescales are especially pivotal to fully understand the photostability and photodamage repair mechanisms in proteins. In 1,2-dithiane, the smallest saturated cyclic molecule that mimics biologically active species with S─S bonds, we investigate the photochemistry upon 200-nm excitation by femtosecond time-resolved x-ray scattering in the gas phase using an x-ray free electron laser. In the femtosecond time domain, we find a very fast reaction that generates molecular fragments with one and two sulfur atoms. On picosecond and nanosecond timescales, a complex network of reactions unfolds that, ultimately, completes the sulfur dissociation from the parent molecule.
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来源期刊
Science Advances
Science Advances 综合性期刊-综合性期刊
CiteScore
21.40
自引率
1.50%
发文量
1937
审稿时长
29 weeks
期刊介绍: Science Advances, an open-access journal by AAAS, publishes impactful research in diverse scientific areas. It aims for fair, fast, and expert peer review, providing freely accessible research to readers. Led by distinguished scientists, the journal supports AAAS's mission by extending Science magazine's capacity to identify and promote significant advances. Evolving digital publishing technologies play a crucial role in advancing AAAS's global mission for science communication and benefitting humankind.
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