Electron transfer photosynthesis

The area of photoinduced electron transfer in LB films has been estabUshed (75). The abiUty to place electron donor and electron acceptor moieties in precise distances allowed the detailed studies of electron-transfer mechanism and provided experimental support for theories (76). This research has been driven by the goal of understanding the elemental processes of photosynthesis. Electron transfer is, however, an elementary process in appHcations such as photoconductivity (77—79), molecular rectification (79—84), etc. 

These are involved in a wide range of electron-transfer processes and in certain oxidation-reduction enzymes, whose function is central to such important processes as the nitrogen cycle, photosynthesis, electron transfer in mitochondria and carbon dioxide fixation. The iron-sulfur proteins display a wide range of redox potentials, from +350 mV in photosynthetic bacteria to —600 mV in chloroplasts. 

Nugent, J.H.A. 1996. Oxygenic photosynthesis Electron transfer in Photosystem I and Photo-system II. Eur. J. Biochem. 237 519-531. 

A photochemically driven reaction that mimics biological photosynthesis, electron-transfer, and hydrocarbon-oxidation reactions is described. The reaction occurs at room temperature and uses 2 as the ultimate oxidant. Most importantly, the reaction can be run for hours without significant degradation. This means that the oxidation of low molecular weight alkanes by O2, which proceeds at a lower rate than for hexane, can be investigated. Further studies are underway to determine the detailed reaction mechanisms involved in the photochemical reaction and the relative contributions of various oxidative pathways. Transient absorption and Raman spectrocopic techniques will also be applied to determine reaction rates. 

Cancer, Topics in Chemical Biology Photosynthesis, Electron Transfer Chemistry in Porphyrin and Corrin Biosynthesis... 

Iron-sulfur clusters are among the most ubiquitous and diverse metal-containing structures in biology. Since the early 1960s they have been known for their role in electron transfer, including most notably in the ferredoxins, the mitochondrial electron transport chain, and photosynthesis.Electron transfer is perhaps the most obvious role for these clusters, due to the presence of at least two redox states readily accessible under normal biological conditions for most types of Fe-S clusters. The role of iron-sulfur clusters in electron transport is covered in detail elsewhere (see Chapter 8.3). 

Levanon H and Mobius K 1997 Advanced EPR spectroscopy on electron transfer processes in photosynthesis and biomimetic model systems Ann. Rev. Biophys. Biomol. Struct. 26 495-540... 

Both PSI and PSII are necessary for photosynthesis, but the systems do not operate in the implied temporal sequence. There is also considerable pooling of electrons in intermediates between the two photosystems, and the indicated photoacts seldom occur in unison. The terms PSI and PSII have come to represent two distinct, but interacting reaction centers in photosynthetic membranes (36,37) the two centers are considered in combination with the proteins and electron-transfer processes specific to the separate centers. 

The Initial Events in Photosynthesis Are Very Rapid Electron-Transfer Reactions... 

What molecular architecture couples the absorption of light energy to rapid electron-transfer events, in turn coupling these e transfers to proton translocations so that ATP synthesis is possible Part of the answer to this question lies in the membrane-associated nature of the photosystems. Membrane proteins have been difficult to study due to their insolubility in the usual aqueous solvents employed in protein biochemistry. A major breakthrough occurred in 1984 when Johann Deisenhofer, Hartmut Michel, and Robert Huber reported the first X-ray crystallographic analysis of a membrane protein. To the great benefit of photosynthesis research, this protein was the reaction center from the photosynthetic purple bacterium Rhodopseudomonas viridis. This research earned these three scientists the 1984 Nobel Prize in chemistry. 

Studies (see, e.g., (101)) indicate that photosynthesis originated after the development of respiratory electron transfer pathways (99, 143). The photosynthetic reaction center, in this scenario, would have been created in order to enhance the efficiency of the already existing electron transport chains, that is, by adding a light-driven cycle around the cytochrome be complex. The Rieske protein as the key subunit in cytochrome be complexes would in this picture have contributed the first iron-sulfur center involved in photosynthetic mechanisms (since on the basis of the present data, it seems likely to us that the first photosynthetic RC resembled RCII, i.e., was devoid of iron—sulfur clusters). 

The many redox reactions that take place within a cell make use of metalloproteins with a wide range of electron transfer potentials. To name just a few of their functions, these proteins play key roles in respiration, photosynthesis, and nitrogen fixation. Some of them simply shuttle electrons to or from enzymes that require electron transfer as part of their catalytic activity. In many other cases, a complex enzyme may incorporate its own electron transfer centers. There are three general categories of transition metal redox centers cytochromes, blue copper proteins, and iron-sulfur proteins. 

Iron-sulfur (Fe-S) proteins function as electron-transfer proteins in many living cells. They are involved in photosynthesis, cell respiration, as well as in nitrogen fixation. Most Fe-S proteins have single-iron (rubredoxins), or two-, three-, or four-iron (ferredoxins), or even seven/eight-iron (nitrogenases) centers. 

Electron transfer reactions constitute an ubiquitous class of chemical reactions. This is particularly true in biological systems where these reactions often occur at interfaces, in photosynthesis for instance. It is therefore challenging to use the surface specificity and the time resolution of the SHG technique to investigate these processes. At liquid-liquid interfaces, these processes are mimicked through the following scheme ... 

Photoinduced ET at liquid-liquid interfaces has been widely recognized as a model system for natural photosynthesis and heterogeneous photocatalysis [114-119]. One of the key aspects of photochemical reactions in these systems is that the efficiency of product separation can be enhanced by differences in solvation energy, diminishing the probability of a back electron-transfer process (see Fig. 11). For instance, Brugger and Gratzel reported that the efficiency of the photoreduction of the amphiphilic methyl viologen by Ru(bpy)3+ is effectively enhanced in the presence of cationic micelles formed by cetyltrimethylammonium chloride [120]. Flash photolysis studies indicated that while the kinetics of the photoinduced reaction,... 

O.G. Poluektov, L.M. Utschig, A.A. Dubinskij and M. Thurnauer, ENDOR of spin-correlated radical pairs in photosynthesis at high magnetic field A tool for mapping electron transfer pathways, J. Am. Chem. Soc., 2004, 126, 1644. 

In biochemical systems, acid-base and redox reactions are essential. Electron transfer plays an obvious, crucial role in photosynthesis, and redox reactions are central to the response to oxidative stress, and to the innate immune system and inflammatory response. Acid-base and proton transfer reactions are a part of most enzyme mechanisms, and are also closely linked to protein folding and stability. Proton and electron transfer are often coupled, as in almost all the steps of the mitochondrial respiratory chain. 

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