文摘
Here, we explore a mechanism of quantum dots related photoreduction of two redox-active proteins, cytochrome c and ferredoxin, by detailed analysis of fluorescence decay and reconstruction of time-resolved emission spectra (TRES). We used two types of cadmium telluride quantum dots, with diameters of 2.6 nm and 3.9 nm and maximum emissions at 550 nm and at 650 nm, respectively, which are known to be able to reduce proteins with different efficiencies. First, we observed that for a pure quantum dots solution, the fluorescence decay can be well fitted by three components. The average fluorescence lifetimes, as well as separate time constants, depend on the nanocrystal diameter. In the presence of proteins, fluorescence decay is faster and cytochrome c has a greater impact than ferredoxin. The TRES experiment showed that a fraction of the medium τ decay component is dominant in a pure quantum dot solution, with the maximum corresponding to the steady-state spectrum. The addition of ferredoxin does not change this pattern, while the presence of cytochrome c strongly promotes the shortest τ. Additionally, potassium iodide titration experiments were used to verify the origin of individual decay components. We propose that reduction occurs by electron transfer from both conductive band and surface trap states.