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arXiv 0902.0389q-bio.BMq-bio.OT
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荧光纳米金刚石用于基于FRET的单一生物纳米荧光素FoF1-ATP合酶的监测

Fluorescent nanodiamonds for FRET-based monitoring of a single biological nanomotor FoF1-ATP synthase

M. Boersch, R. Reuter, G. Balasubramanian, R. Erdmann, F. Jelezko, J. Wrachtrup

摘要:

金刚石纳米晶体中的色心是一类新型荧光标记物,由于无与伦比的亮度、光稳定性和生化惰性而引起人们的极大兴趣。含有缺陷的金刚石纳米晶体可用作标记物,取代传统的有机染料分子、量子点或自体荧光蛋白。它们可以被应用于单个标记的跟踪和超高分辨率定位。此外,金刚石缺陷的自旋特性可以用于具有纳米分辨率的新型磁光成像(MOI)。我们开发这种技术来解开的旋转运动的细节和一个单一的生物纳米FoF 1-ATP合酶的弹性能量存储机制。FoF 1-ATP合成酶是为活细胞提供“化学能量货币”三磷酸腺苷(ATP)的酶。ATP的形成是通过酶内亚基的逐步内部旋转来完成的。以前的亚基旋转已监测单分子荧光共振能量转移(FRET),并受到限制的荧光团的光稳定性。荧光纳米金刚石将这些FRET测量推进到长时间尺度。

英文摘要:

Color centers in diamond nanocrystals are a new class of fluorescence markers that attract significant interest due to matchless brightness, photostability and biochemical inertness. Fluorescing diamond nanocrystals containing defects can be used as markers replacing conventional organic dye molecules, quantum dots or autofluorescent proteins. They can be applied for tracking and ultrahigh-resolution localization of the single markers. In addition the spin properties of diamond defects can be utilized for novel magneto-optical imaging (MOI) with nanometer resolution. We develop this technique to unravel the details of the rotary motions and the elastic energy storage mechanism of a single biological nanomotor FoF1-ATP synthase. FoF1-ATP synthase is the enzyme that provides the 'chemical energy currency' adenosine triphosphate, ATP, for living cells. The formation of ATP is accomplished by a stepwise internal rotation of subunits within the enzyme. Previously subunit rotation has been monitored by single-molecule fluorescence resonance energy transfer (FRET) and was limited by the photostability of the fluorophores. Fluorescent nanodiamonds advance these FRET measurements to long time scales.

机构、总结、中文摘要均由AI分析而来,可能存在错误,请以论文正文为准。

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