Generation of Hydrogen and Oxygen from Water by Solar Energy Conversion

Photosynthesis is considered to be one of the promising areas of cheap and environmentally friendly energy. Photosynthesis involves the process of water oxidation with the formation of molecular oxygen and hydrogen as byproducts. The aim of the present article is to review the energy (light) phase of photosynthesis based on the published X-ray studies of photosystems I and II (PS-I and PS-II). Using modern ideas about semiconductors and biological semiconductor structures, the mechanisms of H+, O2↑, e− generation from water are described. At the initial stage, PS II produces hydrogen peroxide from water as a result of the photoenzymatic reaction, which is oxidized in the active center of PS-II on the Mn4CaO5 cluster to form O2↑, H+, e−. Mn4+ is reduced to Mn2+ and then oxidized to Mn4+ with the transfer of reducing the equivalents of PS-I. The electrons formed are transported to PS-I (P 700), where the electrochemical reaction of water decomposition takes place in a two-electrode electrolysis system with the formation of gaseous oxygen and hydrogen. The proposed functioning mechanisms of PS-I and PS-II can be used in the development of environmentally friendly technologies for the production of molecular hydrogen.

Myelin sheath and cyanobacterial thylakoids as concentric multilamellar structures with similar bioenergetic properties

There is a surprisingly high morphological similarity between multilamellar concentric thylakoids in cyanobacteria and the myelin sheath that wraps the nerve axons. Thylakoids are multilamellar structures, which express photosystems I and II, cytochromes and ATP synthase necessary for the light-dependent reaction of photosynthesis. Myelin is a multilamellar structure that surrounds many axons in the nervous system and has long been believed to act simply as an insulator. However, it has been shown that myelin has a trophic role, conveying nutrients to the axons and producing ATP through oxidative phosphorylation. Therefore, it is tempting to presume that both membranous structures, although distant in the evolution tree, share not only a morphological but also a functional similarity, acting in feeding ATP synthesized by the ATP synthase to the centre of the multilamellar structure. Therefore, both molecular structures may represent a convergent evolution of life on Earth to fulfill fundamentally similar functions.

Non-conventional octameric structure of C-phycocyanin

C-phycocyanin (CPC), a blue pigment protein, is an indispensable component of giant phycobilisomes, which are light-harvesting antenna complexes in cyanobacteria that transfer energy efficiently to photosystems I and II. X-ray crystallographic and electron microscopy (EM) analyses have revealed the structure of CPC to be a closed toroidal hexamer by assembling two trimers. In this study, the structural characterization of non-conventional octameric CPC is reported for the first time. Analyses of the crystal and cryogenic EM structures of the native CPC from filamentous thermophilic cyanobacterium Thermoleptolyngbya sp. O–77 unexpectedly illustrated the coexistence of conventional hexamer and novel octamer. In addition, an unusual dimeric state, observed via analytical ultracentrifugation, was postulated to be a key intermediate structure in the assemble of the previously unobserved octamer. These observations provide new insights into the assembly processes of CPCs and the mechanism of energy transfer in the light-harvesting complexes.

A Transcriptomic Approach to Understanding the Combined Impacts of Supra-Optimal Temperatures and CO2 Revealed Different Responses in the Polyploid Coffea arabica and Its Diploid Progenitor C. canephora

Understanding the effect of extreme temperatures and elevated air (CO2) is crucial for mitigating the impacts of the coffee industry. In this work, leaf transcriptomic changes were evaluated in the diploid C. canephora and its polyploid C. arabica, grown at 25 °C and at two supra-optimal temperatures (37 °C, 42 °C), under ambient (aCO2) or elevated air CO2 (eCO2). Both species expressed fewer genes as temperature rose, although a high number of differentially expressed genes (DEGs) were observed, especially at 42 °C. An enrichment analysis revealed that the two species reacted differently to the high temperatures but with an overall up-regulation of the photosynthetic machinery until 37 °C. Although eCO2 helped to release stress, 42 °C had a severe impact on both species. A total of 667 photosynthetic and biochemical related-DEGs were altered with high temperatures and eCO2, which may be used as key probe genes in future studies. This was mostly felt in C. arabica, where genes related to ribulose-bisphosphate carboxylase (RuBisCO) activity, chlorophyll a-b binding, and the reaction centres of photosystems I and II were down-regulated, especially under 42°C, regardless of CO2. Transcriptomic changes showed that both species were strongly affected by the highest temperature, although they can endure higher temperatures (37 °C) than previously assumed.

Inactivation of mitochondrial Complex I stimulates chloroplast ATPase in Physcomitrella (Physcomitrium patens)

While light is the ultimate source of energy for photosynthetic organisms, mitochondrial respiration is still fundamental for supporting metabolism demand during the night or in heterotrophic tissues. Respiration is also important for the metabolism of photosynthetically active cells, acting as a sink for excess reduced molecules and source of substrates for anabolic pathways. In this work, we isolated Physcomitrella (Physcomitrium patens) plants with altered respiration by inactivating Complex I of the mitochondrial electron transport chain by independent targeting of two essential subunits. Results show that the inactivation of Complex I causes a strong growth impairment even in fully autotrophic conditions in tissues where all cells are photosynthetically active. Complex I mutants show major alterations in the stoichiometry of respiratory complexes while the composition of photosynthetic apparatus was substantially unaffected. Complex I mutants showed altered photosynthesis with higher yields of both Photosystems I and II. These are the consequence of a higher chloroplast ATPase activity that also caused a smaller ΔpH formation across thylakoid membranes as well as decreased photosynthetic control on cytochrome b6f, possibly to compensate for a deficit in ATP supply relative to demand in Complex I mutants. These results demonstrate that alteration of respiratory activity directly impacts photosynthesis in P. patens and that metabolic interaction between organelles is essential in their ability to use light energy for growth.

Hybrid Electrophototroph Enables High-Efficiency Carbon Dioxide Valorization to Fuel Molecules

Nature’s biocatalytic processes are driven by photosynthesis, whereby photosystems I and II are connected in series for light-stimulated generation of fuel products or electricity. Externally supplying electricity directly to the photosynthetic electron transfer chain (PETC) has numerous potential benefits, although strategies for achieving this goal have remained elusive. Here we report an integrated photo-electrochemical architecture which shuttles electrons directly to PETC in living cyanobacteria. The cathode of this architecture electrochemically interfaces with cyanobacterial cells lacking photosystem II activity that cannot perform photosynthesis independently. Illumination of the cathode channels electrons from external circuit to intracellular PETC through photosystem I, ultimately fueling CO2 conversion to acetate, a model fuel molecule with 9.32% energy efficiency, exceeding the efficiency of natural photosynthesis in higher plants (<1%) and cyanobacteria (~4-7%). The resulting “Electrophototrophic” bio-electrochemical hybrid has the potential to produce fuel chemicals with numerous advantages over standalone natural and artificial photosynthetic approaches.