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首页> 外文期刊>Applied Magnetic Resonance >Effect of a Protein on the Light Energy Conversion in Dual Fluorophore-Nitroxide Probes Studied by ESR and Fluorescence
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Effect of a Protein on the Light Energy Conversion in Dual Fluorophore-Nitroxide Probes Studied by ESR and Fluorescence

机译：ESR和荧光研究蛋白质对双荧光团-一氧化氮探针光能转换的影响

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摘要

Probing biological environment with dual fluorophore-nitroxide (FN) molecules in which fluorophore is tethered with nitroxide, a fluorescence quencher, opens unique opportunities to study molecular dynamics and micropolarity of the medium which affect intramolecular fluorescence quenching (IFQ), electron transfer, photoreduction and light energy conversion. In such molecules, the excited fragment of the chromophore can serve as an electron donor, and the nitroxide fragment as an electron acceptor. The same groups allow monitoring of molecular dynamics and also make it possible to measure micropolarity of the medium in the vicinity of the donor (by fluorescence technique) and acceptor (by electron spin resonance [ESR]) moieties. In the present work, two dual dansylnitroxide probes were incorporated in a binding site of bovine serum albumin. Their interactions with the protein, mobility, and photoreduction, as well as micropolarity of the media, have been studied by ESR and fluorescence methods. IFQ and spectral relaxation shift of the dansyl fragment have been monitored by time-resolved fluorescence technique. In parallel, computational studies on intramolecular dynamics of the FN probe were performed. On the basis of the Marcus model of the electron transfer between the excited dansyl fluorophore (donor) and nitroxide group (acceptor) and our experimental data, the mechanism of the electron transfer in the dual molecules incorporated into bovine serum albumin was established. It was shown that dual FN molecules in the protein meet main requirements for an efficient light energy conversion system.
机译：用双荧光团氮氧化物（FN）分子探测生物环境，其中荧光团与荧光猝灭剂一氧化氮束缚在一起，为研究影响分子内荧光猝灭（IFQ），电子转移，光还原和光能转换。在这样的分子中，发色团的激发片段可以用作电子给体，而氮氧化物片段可以用作电子受体。相同的组可以监测分子动力学，也可以测量供体（通过荧光技术）和受体（通过电子自旋共振[ESR]）部分附近介质的微极性。在目前的工作中，两个双重丹磺酰硝基探针被掺入到牛血清白蛋白的结合位点。通过ESR和荧光方法研究了它们与蛋白质的相互作用，迁移率，光还原以及介质的微极性。通过时间分辨荧光技术监测了丹磺酰基片段的IFQ和光谱弛豫位移。并行地，进行了关于FN探针的分子内动力学的计算研究。基于激发的丹磺酰基荧光团（供体）与一氧化氮基团（受体）之间电子转移的Marcus模型和我们的实验数据，建立了掺入牛血清白蛋白的双分子中电子转移的机理。结果表明，蛋白质中的双FN分子满足了高效光能转换系统的主要要求。

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