Photosystem I

Kothe G, Weber S, BittI R, Ohmes E, Thurnauer M and Norris J 1991 Transient EPR of light-induced radical pairs in plant photosystem I observation of quantum beats Chem. Rhys. Lett. 186 474-80... 

The electrons undergo the equivalent of a partial oxidation process ia a dark reaction to a positive potential of +0.4 V, and Photosystem I then raises the potential of the electrons to as high as —0.7 V. Under normal photosynthesis conditions, these electrons reduce tryphosphopyridine-nucleotide (TPN) to TPNH, which reduces carbon dioxide to organic plant material. In the biophotolysis of water, these electrons are diverted from carbon dioxide to a microbial hydrogenase for reduction of protons to hydrogen ... 

Electron Transport Between Photosystem I and Photosystem II Inhibitors. The interaction between PSI and PSII reaction centers (Fig. 1) depends on the thermodynamically favored transfer of electrons from low redox potential carriers to carriers of higher redox potential. This process serves to communicate reducing equivalents between the two photosystem complexes. Photosynthetic and respiratory membranes of both eukaryotes and prokaryotes contain stmctures that serve to oxidize low potential quinols while reducing high potential metaHoproteins (40). In plant thylakoid membranes, this complex is usually referred to as the cytochrome b /f complex, or plastoquinolplastocyanin oxidoreductase, which oxidizes plastoquinol reduced in PSII and reduces plastocyanin oxidized in PSI (25,41). Some diphenyl ethers, eg, 2,4-dinitrophenyl 2 -iodo-3 -methyl-4 -nitro-6 -isopropylphenyl ether [69311-70-2] (DNP-INT), and the quinone analogues,... 

Golbeck, / H., 1992. Structure and fnncdon of photosystem I. Annual Review of Plant Physiology and Plant Molecular Biology 43 292—324. 

Kranss, N., et al., 1996. Photosystem I at 4 A resolution represents the first structural model of a joint photosynthedc reaction centre and core antenna system. Nature Structural Biology 3 965-973. 

In 1987, the iron-sulfur clusters Fa and Fb acting as terminal electron acceptors in photosystem I have been shown to be located on a... 

Clusters Fa and Fb of photosystem I from cyanobacteria and chloro-plasts are distinguished by their EPR signatures (26, 27) and their reduction potentials (-520 mV for Fa and -580 mV for Fb Ref. (28). The assignment of cysteines in the primary sequence as ligands to individual clusters has been achieved by site-specific mutagenesis (29, Fig. 3), and structural information with regard to the environment of both clusters has been obtained by NMR (24). 

Mullineaux, C. W. (1992). Excitation energy transfer from phycobilisomes to photosystem-I in a cyanobacterium. Biochim Biophys Acta 1100(3) 285-292. 

Rakhimberdieva, M. G., V. A. Boichenko, N. V. Karapetyan, and I. N. Stadnichuk (2001). Interaction of phy-cobilisomes with photosystem B dimers and photosystem I monomers and trimers in the cyanobacterium Spirulina platensis. Biochemistry 40(51) 15780-15788. 

The g-tensor principal values of radical cations were shown to be sensitive to the presence or absence of dimer- and multimer-stacked structures (Petrenko et al. 2005). If face-to-face dimer structures occur (see Scheme 9.7), then a large change occurs in the gyy component compared to the monomer structure. DFT calculations confirm this behavior and permitted an interpretation of the EPR measurements of the principal g-tensor components of the chlorophyll dimers with stacked structures like the P 00 special dimer pair cation radical and the P700 special dimer pair triplet radical in photosystem I. Thus dimers that occur for radical cations can be deduced by monitoring the gyy component. 

Fig. 5.8. When photosystem II is activated by absorbing photons, electrons are passed along an electron-acceptor chain and are eventually donated to photosystem I and finally to NAPD+. Photosystem II is responsible for the photolytic dissociation of water and the production of atmospheric oxygen. This pathway is sometimes referred to as the Z scheme because of its zigzag route, as depicted here, but the two arms are in fact remote in space. (Note Plastocyanin (Cu) is an alternative late replacement for an Fe cytochrome complex).

When a trichome moves into a photosystem I light trap, electrons are drained out of the pool. In both cases a phobic response is caused, but different patterns result, one being an accumulation in, the other a dispersal from, the light trap l0]). 

In photosystem I, absorption of a photon leads to an excited state that functions as a reducing agent. The electrons are passed from one species to another with several intermediate species that include ferrodoxin (a protein containing iron and sulfur) before finally reducing C02. In photosystem II, electrons are transferred to a series of intermediates, of which a cytochrome bf complex is one entity. Ultimately, the transfer of electrons leads to the reaction... 

The reaction-center proteins for Photosystems I and II are labeled I and II, respectively. Key Z, the watersplitting enzyme which contains Mn P680 and Qu the primary donor and acceptor species in the reaction-center protein of Photosystem II Qi and Qt, probably plastoquinone molecules PQ, 6-8 plastoquinone molecules that mediate electron and proton transfer across the membrane from outside to inside Fe-S (an iron-sulfur protein), cytochrome f, and PC (plastocyanin), electron carrier proteins between Photosystems II and I P700 and Au the primary donor and acceptor species of the Photosystem I reaction-center protein At, Fe-S a and FeSB, membrane-bound secondary acceptors which are probably Fe-S centers Fd, soluble ferredoxin Fe-S protein and fp, is the flavoprotein that functions as the enzyme that carries out the reduction of NADP+ to NADPH. 

The primary donor in Photosystem I P700 is thought to be a special pair of chlorophyll a molecules. Katz and Hindman (18) have reviewed a number of systems designed to mimic the properties of P700 ranging from chlorophyll a in certain solvents under special conditions where dimers form spontaneously (19) to covalently linked chlorophylls (20). Using these models it has been possible to mimic many of the optical, EPR and redox properties of the in vivo P700 entity. 

Although studied in great detail, the action of chlorophyll is still not fully understood however, steady progress towards a more complete understanding has taken place over the past several decades. Two photosynthetic systems (photosystems I and II) are present in green plants - each incorporating a different chlorophyll type. When a photon is absorbed by a chlorophyll molecule, its energy is transformed and... 

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