Highly effi cient light absorption and charge separation within the photosystem and reaction center (RC) complexes of photosynthetic plants and bacteria are of great interest for solar cell and photo detector applications, since they offer almost unity quantum yield and expected ultimate power conversion effi ciencies of more than 18% and 12%, respectively. In addition, the charge separated states created by these protein complexes are very long lived compared to conventional semiconductor solar cells. In this work, a novel technique is presented for the deposition of photosynthetic protein complexes, by electrospraying RCs of Rhodobacter sphaeroides onto highly ordered pyrolytic graphite (HOPG) electrodes. Remarkably, it is shown that the RCs not only survive exposure to the high electric fi elds but also yield peak photocurrent densities of up to 7 µA cm −2 , which is equal to the highest value reported to date.

Abstract:The performance of bio-photovoltaic devices with a monolayer of the immobilized photosynthetic reaction center (RC) is generally low because of weak light absorption and poor charge transfer between the RC and the electrode. In this paper, a new bio-photovoltaic device is described in which the RC is dissolved in the electrolyte of an electrochemical cell. The charges generated by the illuminated RC are transferred to electrodes via mediators. The difference between the reaction rates of two types of mediator at the electrode surfaces determines the direction of the photocurrent in the device. Experimental results show that the magnitude of the photocurrent is proportional to the incident light intensity, and the current increases nonlinearly with an increase in the RC concentration in the electrolyte. With further optimization this approach should lead to devices with improved light absorption.

Photosynthetic reaction centres (RCs) convert light into separated charges with nearly perfect quantum efficiency, and have been used to generate photocurrent. Previous work has shown that electron tunnelling rates between redox centres in proteins depend exponentially on the tunnelling distance. In this work the RC from Rhodobacter sphaeroides was genetically modified with the aim of achieving the shortest tunnelling distances yet demonstrated between the RC's electron-accepting P site and underlying graphite and gold electrodes, and between the electron donor Q site and graphite electrodes. Opposite charges are carried to counter electrodes using mobile mediators, as in dye-sensitised solar cells. Native RCs are bound to graphite surfaces through N-(1-pyrene)iodoacetamide. Although the linker's length is only 4 Å, the electron transfer pathway between the Q electron donor site on the RC and the electrode surface is still too large for current to be significant. A mutant version with the electron acceptor P side close to the graphite surface produced currents of 15 nA cm −2 upon illumination. Direct binding of RCs to a gold surface is shown, resulting in currents of 5 nA cm −2 . In both cases the current was unaffected by mediator concentration but increased with illumination, suggesting that direct electron transfer was achieved. The engineering of an RC to achieve direct electron transfer will help with long term efforts to demonstrate RC-based photovoltaic devices.

We address a challenge in the engineering of proteins to redirect electron transfer pathways, using the bacterial photosynthetic reaction centre (RC) pigment-protein complex. Direct electron transfer is shown to occur from the Q quinone of the Rhodobacter sphaeroides RC containing a truncated H protein and bound on the quinone side to a gold electrode. In previous reports of binding to the quinone side of the RC, electron transfer has relied on the use of a soluble mediator between the RC and an electrode, in part because the probability of Q quinone reduction is much greater than that of direct electron transfer through the large cytoplasmic domain of the H subunit, presenting a ~ 25 Å barrier. A series of C-terminal truncations of the H subunit were created to expose the quinone region of the RC L and M proteins, and all truncated RC H mutants assembled in vivo. The 45M mutant was designed to contain only the N-terminal 45 amino acid residues of the H subunit including the membrane-spanning α-helix; the mutant RC was stable when purified using the detergent N-dodecyl-β-D-maltoside, contained a near-native ratio of bacteriochlorophylls to bacteriopheophytins, and showed a charge-separated state of [Formula: see text]. The 45M-M229 mutant RC had a Cys residue introduced in the vicinity of the Q quinone on the newly exposed protein surface for electrode attachment, decreasing the distance between the quinone and electrode to ~ 12 Å. Steady-state photocurrents of up to around 200 nA/cm were generated in the presence of 20 mM hydroquinone as the electron donor to the RC. This novel configuration yielded photocurrents orders of magnitude greater than previous reports of electron transfer from the quinone region of RCs bound in this orientation to an electrode.

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