| 研究実績の概要 |
Within the past year, we have increased our insight into our transient protein photodetectors, based on the metal, protein, liquid insulator, metal architecture, using the thermophilic photoactive microbial rhodopsin TR. Using this protein we could enhance the detectivity of our protein photodetectors by an order of magnitude compared to our prototype photodetectors using the sensory rhodopsin SrSRI. The stable and comparably strong signal allowed us to further characterise the photodetector performance in terms of bandwidth and wavelength dependence, which followed the shape of the absorption spectra of TR. Furthermore, due to its high thermal stability, we could increase the bandwidth of our photodetectors further by increasing the temperature to 70C, the native environment of the protein, at which the protein was expected to have its optimal photoresponse. This platform further enabled us to study the effect of the protein environment in the films, suggesting that an increased ionic content improves the signal strength, as does the film homogeneity, which could be optimised throughout the study. The correlation of the wavelength dependence and temperature dependence to the intrinsic properties of the protein strongly supports the influence of the protein on the photodetectors performance, which shows the benefit of the semiliquid architecture of these photodetectors.
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