Redox heme-proteins mediated fluorescence of CdSe/ZnS quantum dots

被引：3

作者：

Qin, Lixia ^{[1
]}

He, Luwei ^{[1
]}

Ji, Congcong ^{[1
]}

Li, Xiangqing ^{[1
]}

Kang, Shi-Zhao ^{[1
]}

Mu, Jin ^{[1
]}

机构：

[1] Shanghai Inst Technol, Sch Chem & Environm Engn, Shanghai 201418, Peoples R China

来源：

JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY | 2014年 / 133卷

基金：

中国国家自然科学基金;

关键词：

Redox proteins; Quantum dots; Electrostatic interactions; Spectroelectrochemistry; Fluorescence imaging; ULTRAFAST ELECTRON-TRANSFER; CYTOCHROME-C; LIGAND-EXCHANGE; NANOPARTICLES; SENSORS; THERMODYNAMICS; RADICALS; CDTE;

D O I：

10.1016/j.jphotobiol.2014.02.017

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The redox properties of cytochrome c (Cyt c), hemoglobin (Hb) and myoglobin (Mb) were studied based on electrostatic interactions between Thioglycolic acid (TGA) capped CdSe/ZnS quantum dots (QDs) and proteins. Results indicated that only Cyt c quenched the fluorescence of the QDs at pH > 8.0. Under the optimized conditions, a significant fluorescence recovery of the QDs' system was observed when the reduced form of Cyt c incubated with TGA capped QDs, however, the reduced state of Hb and Mb resulted in a more fluorescence quenching on the same size of QDs. Interestingly, the fluorescence changes of QDs-proteins could be switched by modulating the redox potentials of proteins-attached QDs. Moreover, only the oxidized Cyt c form was reduced by the generated O-2(.-), that significantly enhanced the fluorescence of the QDs' system, which was also demonstrated by fluorescence imaging in HeLa cells. (C) 2014 Elsevier B.V. All rights reserved.

引用

页码：65 / 72

页数：8

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