Redox heme-proteins mediated fluorescence of CdSe/ZnS quantum dots.
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 O2(-) that significantly enhanced the fluorescence of the QDs' system, which was also demonstrated by fluorescence imaging in HeLa cells.
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, 100 Haiquan Road, Shanghai 201418, China.
Lixia
L
Qin
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, 100 Haiquan Road, Shanghai 201418, China.
Luwei
L
He
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, 100 Haiquan Road, Shanghai 201418, China.
Congcong
C
Ji
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, 100 Haiquan Road, Shanghai 201418, China.
Xiangqing
X
Li
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, 100 Haiquan Road, Shanghai 201418, China.
Shi-Zhao
SZ
Kang
School of Chemical and Environmental Engineering, Shanghai Institute of Technology, 100 Haiquan Road, Shanghai 201418, China. Electronic address: mujin@sit.edu.cn.
Jin
J
Mu
D019187:Cadmium Compounds / Q000737:chemistry; D045304:Cytochromes c / Q000737:chemistry* / Q000378:metabolism; D006367:HeLa Cells; D006454:Hemoglobins / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D018613:Microscopy, Confocal; D009211:Myoglobin / Q000737:chemistry* / Q000378:metabolism; D010084:Oxidation-Reduction; D045663:Quantum Dots / Q000737:chemistry*; D018036:Selenium Compounds / Q000737:chemistry; D013050:Spectrometry, Fluorescence; D013440:Sulfides / Q000737:chemistry; D013864:Thioglycolates / Q000737:chemistry; D017967:Zinc Compounds / Q000737:chemistry
D019187:Cadmium Compounds; D006454:Hemoglobins; D009211:Myoglobin; D018036:Selenium Compounds; D013440:Sulfides; D013864:Thioglycolates; D017967:Zinc Compounds; C017487:2-mercaptoacetate; D045304:Cytochromes c; C058667:cadmium selenide; C031238:zinc sulfide
Electrostatic interactions; Fluorescence imaging; Quantum dots; Redox proteins; Spectroelectrochemistry