Unequal misses during the flash-induced advancement of photosystem II: effects of the S state and acceptor side cycles.

Photosynthetic water oxidation is catalyzed by the oxygen-evolving complex (OEC) in photosystem II (PSII). This process is energetically driven by light-induced charge separation in the reaction center of PSII, which leads to a stepwise accumulation of oxidizing equivalents in the OEC (Si states, i = 0-4) resulting in O2 evolution after each fourth flash, and to the reduction of plastoquinone to plastoquinol on the acceptor side of PSII. However, the Si-state advancement is not perfect, which according to the Kok model is described by miss-hits (misses). These may be caused by redox equilibria or kinetic limitations on the donor (OEC) or the acceptor side. In this study, we investigate the effects of individual S state transitions and of the quinone acceptor side on the miss parameter by analyzing the flash-induced oxygen evolution patterns and the S2, S3 and S0 state lifetimes in thylakoid samples of the extremophilic red alga Cyanidioschyzon merolae. The data are analyzed employing a global fit analysis and the results are compared to the data obtained previously for spinach thylakoids. These two organisms were selected, because the redox potential of QA/QA- in PSII is significantly less negative in C. merolae (Em = - 104 mV) than in spinach (Em = - 163 mV). This significant difference in redox potential was expected to allow the disentanglement of acceptor and donor side effects on the miss parameter. Our data indicate that, at slightly acidic and neutral pH values, the Em of QA-/QA plays only a minor role for the miss parameter. By contrast, the increased energy gap for the backward electron transfer from QA- to Pheo slows down the charge recombination reaction with the S3 and S2 states considerably. In addition, our data support the concept that the S2 → S3 transition is the least efficient step during the oxidation of water to molecular oxygen in the Kok cycle of PSII.

A single residue can modulate nanocage assembly in salt dependent ferritin.

Cage forming proteins have numerous potential applications in biomedicine and biotechnology, where the iron storage ferritin is a widely used example. However, controlling ferritin cage assembly/disassembly remains challenging, typically requiring extreme conditions incompatible with many desirable cargoes, particularly for more fragile biopharmaceuticals. Recently, a ferritin from the hyperthermophile bacterium Thermotoga maritima (TmFtn) has been shown to have reversible assembly under mild conditions, offering greater potential biocompatibility in terms of cargo access and encapsulation. Like Archeoglobus fulgidus ferritin (AfFtn), TmFtn forms 24mer cages mediated by metal ions (Mg2+). We have solved the crystal structure of the wild type TmFtn and several mutants displaying different assembly/disassembly properties. These data combined with other biophysical studies allow us to suggest candidate interfacial amino acids crucial in controlling assembly. This work deepens our understanding of how these ferritin complexes assemble and is a useful step towards production of triggerable ferritins in which these properties can be finely designed and controlled.

Plasmon-induced absorption of blind chlorophylls in photosynthetic proteins assembled on silver nanowires.

We demonstrate that controlled assembly of eukaryotic photosystem I with its associated light harvesting antenna complex (PSI-LHCI) on plasmonically active silver nanowires (AgNWs) substantially improves the optical functionality of such a novel biohybrid nanostructure. By comparing fluorescence intensities measured for PSI-LHCI complex randomly oriented on AgNWs and the results obtained for the PSI-LHCI/cytochrome c553 (cyt c553) bioconjugate with AgNWs we conclude that the specific binding of photosynthetic complexes with defined uniform orientation yields selective excitation of a pool of chlorophyll (Chl) molecules that are otherwise almost non-absorbing. This is remarkable, as this study shows for the first time that plasmonic excitations in metallic nanostructures can not only be used to enhance native absorption of photosynthetic pigments, but also - by employing cyt c553 as the conjugation cofactor - to activate the specific Chl pools as the absorbing sites only when the uniform and well-defined orientation of PSI-LHCI with respect to plasmonic nanostructures is achieved. As absorption of PSI alone is comparatively low, our approach lends itself as an innovative approach to outperform the reported-to-date biohybrid devices with respect to solar energy conversion.

A quest for the artificial leaf.

It has been estimated that the energy captured in one hour of sunlight that reaches our planet is equivalent to annual energy production by human population globally. To efficiently capture the practically inexhaustible solar energy and convert it into high energy density solar fuels provides an attractive 'green' alternative to running our present day economies on rapidly depleting fossil fuels, especially in the context of ever growing global energy demand. Natural photosynthesis represents one of the most fundamental processes that sustain life on Earth. It provides nearly all the oxygen we breathe, the food we consume and fossil fuels that we so much depend on. Imitating the reactions that occur at the early stages of photosynthesis represents the main challenge in the quest for construction of an efficient, robust, self-renewing and cost-effective 'artificial leaf'. In this review we summarize the main molecular features of the natural solar energy converters, photosystem I and photosystem II, that allow them to operate at high quantum efficiencies, and thus inspire the smart matrix design of the artificial solar-to-fuel devices. We also discuss the main challenges that face the field and overview selected recent technological advances that have tremendously accelerated the race for a fully operational artificial leaf that could serve as a viable alternative to fossil fuels for energy production.

Structure and function of photosystem I and its application in biomimetic solar-to-fuel systems.

Photosystem I (PSI) is one of the most efficient biological macromolecular complexes that converts solar energy into condensed energy of chemical bonds. Despite high structural complexity, PSI operates with a quantum yield close to 1.0 and to date, no man-made synthetic system approached this remarkable efficiency. This review highlights recent developments in dissecting molecular structure and function of the prokaryotic and eukaryotic PSI. It also overviews progress in the application of this complex as a natural photocathode for production of hydrogen within the biomimetic solar-to-fuel nanodevices.