Abstract
Bio-dyes for light harvesting in dye-sensitized solar cells (DSSC) have the advantage of being environmentally-friendly, non-toxic alternatives, which can be produced in a sustainable fashion. Free photosynthetic pigments are unstable in the presence of light and oxygen, a situation which can hardly be avoided during the operation of DSSCs, especially in large-scale applications. We therefore investigated the recombinant light-harvesting protein LHCBM6, which naturally occurs in the photosynthetic apparatus of the green microalga Chlamydomonas reinhardtii as a bio-dye in DSSCs. Photocurrent densities of up to 0.87 and 0.94 mA·cm−2 were determined for the DSSCs and solar energy to electricity conversion efficiencies (η) reached about 0.3% (100 mW·cm−2; AM 1.5 G filter applied). Importantly, we observed an unprecedented stability of LHCII-based DSSCs within long DSSC operation times of at least 7 days in continuous light and show that operation times are restricted by electrolyte decomposition rather than reduced dye performance, as could be demonstrated by DSSC reactivation following re-supplementation with fresh electrolyte. To the best of our knowledge, this is the first study analysing bio-dye sensitized DSSCs over such long periods, which revealed that during illumination an activation of the DSSCs occurs.
Highlights
Oxygenic photosynthesis can be sub-divided into two major types of biochemical reactions
Excitation energy transfer towards the special pair chlorophyll of the PSII reaction centre (P680), whose excitation is followed by charge separation reactions and electron transfer to the electron carrier plastoquinone[2,3], requires chlorophyll a and b as well as carotenoids bound to LHCII apoproteins
We investigated whether recombinant LHCBM6 from the green microalga Chlamydomonas reinhardtii represents a suitable bio-dye in dye-sensitized solar cells (DSSC) applications
Summary
Oxygenic photosynthesis can be sub-divided into two major types of biochemical reactions. Comparison of the absorbance spectra indicated that the lower phase contains properly refolded LHCBM6 protein, which was further confirmed by recording fluorescence emission spectra of both fractions after excitation at 440 nm, 475 nm and 500 nm (Fig. 2B, C).
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