Primary Electron Acceptor Research Articles

Chloroplast-encoded Polypeptide PsbT Is Involved in the Repair of Primary Electron Acceptor QA of Photosystem II during Photoinhibition in Chlamydomonas reinhardtii

PsbT is a small chloroplast-encoded hydrophobic polypeptide associated with the D1/D2 heterodimer of the photosystem II (PSII) reaction center and is required for the efficient post-translational repair of photodamaged PSII. Here we addressed that role in detail in Chlamydomonas reinhardtii wild type and DeltapsbT cells by analyzing the activities of PSII, the assembly of PSII proteins, and the redox components of PSII during photoinhibition and repair. Strong illumination of cells for 15 min decreased the activities of electron transfer through PSII and Q(A) photoreduction by 50%, and it reduced the amount of atomic manganese by 20%, but it did not affect the steady-state level of PSII proteins, photoreduction of pheophytin (pheo(D1)), and the amount of bound plastoquinone (Q(A)), indicating that the decrease in PSII activity resulted mainly from inhibition of the electron transfer from pheo(D1) to Q(A). In wild type cells, we observed parallel recovery of electron transfer activity through PSII and Q(A) photoreduction, suggesting that the recovery of Q(A) activity is one of the rate-limiting steps of PSII repair. In DeltapsbT cells, the repairs of electron transfer activity through PSII and of Q(A) photoreduction activity were both impaired, but PSII protein turnover was unaffected. Moreover, about half the Q(A) was lost from the PSII core complex during purification. Since PsbT is intimately associated with the Q(A)-binding region on D2, we propose that this polypeptide enhances the efficient recovery of Q(A) photoreduction by stabilizing the structure of the Q(A)-binding region.

Radiative and non-radiative charge recombination pathways in Photosystem II studied by thermoluminescence and chlorophyll fluorescence in the cyanobacterium Synechocystis 6803

The mechanism of charge recombination was studied in Photosystem II by using flash induced chlorophyll fluorescence and thermoluminescence measurements. The experiments were performed in intact cells of the cyanobacterium Synechocystis 6803 in which the redox properties of the primary pheophytin electron acceptor, Phe, the primary electron donor, P 680, and the first quinone electron acceptor, Q A, were modified. In the D1Gln130Glu or D1His198Ala mutants, which shift the free energy of the primary radical pair to more positive values, charge recombination from the S 2Q A − and S 2Q B − states was accelerated relative to the wild type as shown by the faster decay of chlorophyll fluorescence yield, and the downshifted peak temperature of the thermoluminescence Q and B bands. The opposite effect, i.e. strong stabilization of charge recombination from both the S 2Q A − and S 2Q B − states was observed in the D1Gln130Leu or D1His198Lys mutants, which shift the free energy level of the primary radical pair to more negative values, as shown by the retarded decay of flash induced chlorophyll fluorescence and upshifted thermoluminescence peak temperatures. Importantly, these mutations caused a drastic change in the intensity of thermoluminescence, manifested by 8- and 22-fold increase in the D1Gln130Leu and D1His198Lys mutants, respectively, as well as by a 4- and 2.5-fold decrease in the D1Gln130Glu and D1His198Ala mutants, relative to the wild type, respectively. In the presence of the electron transport inhibitor bromoxynil, which decreases the redox potential of Q A/Q A − relative to that observed in the presence of DCMU, charge recombination from the S 2Q A − state was accelerated in the wild type and all mutant strains. Our data confirm that in PSII the dominant pathway of charge recombination goes through the P 680 +Phe − radical pair. This indirect recombination is branched into radiative and non-radiative pathways, which proceed via repopulation of P 680 * from 1[P 680 +Ph −] and direct recombination of the 3[P 680 +Ph −] and 1[P 680 +Ph −] radical states, respectively. An additional non-radiative pathway involves direct recombination of P 680 +Q A −. The yield of these charge recombination pathways is affected by the free energy gaps between the Photosystem II electron transfer components in a complex way: Increase of Δ G(P 680 * ↔ P 680 +Phe −) decreases the yield of the indirect radiative pathway (in the 22–0.2% range). On the other hand, increase of Δ G(P 680 +Phe − ↔ P 680 +Q A −) increases the yield of the direct pathway (in the 2–50% range) and decreases the yield of the indirect non-radiative pathway (in the 97–37% range).

Replacement of the methionine axial ligand to the primary electron acceptor A 0 slows the A 0− reoxidation dynamics in Photosystem I

The recent crystal structure of photosystem I (PSI) from Thermosynechococcus elongatus shows two nearly symmetric branches of electron transfer cofactors including the primary electron donor, P 700, and a sequence of electron acceptors, A, A 0 and A 1, bound to the PsaA and PsaB heterodimer. The central magnesium atoms of each of the putative primary electron acceptor chlorophylls, A 0, are unusually coordinated by the sulfur atom of methionine 688 of PsaA and 668 of PsaB, respectively. We [Ramesh et al. (2004a) Biochemistry 43:1369–1375] have shown that the replacement of either methionine with histidine in the PSI of the unicellular green alga Chlamydomonas reinhardtii resulted in accumulation of A 0 − (in 300-ps time scale), suggesting that both the PsaA and PsaB branches are active. This is in contrast to cyanobacterial PSI where studies with methionine-to-leucine mutants show that electron transfer occurs predominantly along the PsaA branch. In this contribution we report that the change of methionine to either leucine or serine leads to a similar accumulation of A 0 − on both the PsaA and the PsaB branch of PSI from C. reinhardtii, as we reported earlier for histidine mutants. More importantly, we further demonstrate that for all the mutants under study, accumulation of A 0 − is transient, and that reoxidation of A 0 − occurs within 1–2 ns, two orders of magnitude slower than in wild type PSI, most likely via slow electron transfer to A 1. This illustrates an indispensable role of methionine as an axial ligand to the primary acceptor A 0 in optimizing the rate of charge stabilization in PSI. A simple energetic model for this reaction is proposed. Our findings support the model of equivalent electron transfer along both cofactor branches in Photosystem I.

Laboratory-Scale Iron EDTA-Based NOX Scrubbing Process with Biological Treatment and Regeneration of Spent Scrubber Water

A laboratory-scale apparatus was configured and operated to evaluate the efficacy of a unit process that integrates the absorption of nitric oxide in an aqueous solution of ferrous ethylenediaminetetraacetic acid (EDTA), with biological treatment and regeneration by reduction of oxidized species in that solution. The reactor was initially inoculated with anoxic denitrifying and strictly anaerobic biomass from two municipal wastewater treatment plants. After successful development of biomass using nitrate and ferric EDTA as the primary electron acceptors and ethanol as the primary electron donor, the system was modified to continuously load nitric oxide in the form of the nitrosyl adduct of ferrous EDTA. The process was operated in this manner for 107 days, including a steady-state period that was maintained for more than 70 days. During the period of steady-state operation, 0.194 mol of NO and 0.166 mol of ethanol were loaded per day. This corresponded with biogas formation at a consistent rate (0.669 lit...

Photophysical studies of supramolecular triads involving zinc naphthalocyanines and pyridylfullerenes with a second electron donor

Supramolecular triads composed of zinc naphthalocyanine ( ZnNc ) as an electron donor, pyridylfullerenes as primary electron acceptors, and either ferrocene ( Fc ) or N , N -dimethylaminophenyl ( DMA ) entities as second electron donors were constructed via metal-ligand axial coordination. The formation of the supramolecular triads was monitored using optical absorption methods and the measured binding constants revealed a moderately stable complex formation. The B3LYP/3-21G(*) optimized structures showed the disposition of the three entities of the triads to be in a linear fashion. The redox behavior of the different components was studied using cyclic voltammetry in o-dichlorobenzene containing (n- C 4 H 9)4 NClO 4. The donor ability evaluated from the oxidation potentials of the electron donors followed the trend: ZnNc < Fc < DMA . Efficient electron transfer from the excited singlet state of zinc naphthalocyanine to the fullerene entity was observed in all of the studied triads in o-dichlorobenzene by fluorescence quenching measurements. Clear evidence, that the charge-separation process formed the radical ions in the triads, was obtained from a nanosecond transient absorption spectral technique, indicating the contribution of the second electron donor in prolonging the charge-separated states.

Kinetics of a hydrogen-oxidizing, perchlorate-reducing bacterium

This paper provides the first kinetic parameters for a hydrogen-oxidizing perchlorate-reducing bacterium (PCRB), Dechloromonas sp. PC1. The q max for perchlorate and chlorate were 3.1 and 6.3 mg/mgDW-day, respectively. The K for perchlorate was 0.14 mg/L, an order of magnitude lower than reported for other PCRB. The yields Y on perchlorate and chlorate were 0.23 and 0.22 mgDW/mg, respectively, and the decay constant b was 0.055/day. The growth-threshold, S min, for perchlorate was 14 μg/L, suggesting that perchlorate cannot be reduced below this level when perchlorate is the primary electron-acceptor, although it may be possible when oxygen or nitrate is the primary acceptor. Chlorate accumulated at maximum concentrations of 0.6–4.3 mg/L in batch tests with initial perchlorate concentrations ranging from 100 to 600 mg/L. Furthermore, 50 mg/L chlorate inhibited perchlorate reduction with perchlorate at 100 mg/L. This is the first report of chlorate accumulation and inhibition for a pure culture of PCRB. These Chlorate effects are consistent with competitive inhibition between perchlorate and chlorate for the (per)chlorate reductase enzyme.

Selective detection of the structural changes upon photoreactions of several redox cofactors in photosystem II by means of light-induced ATR-FTIR difference spectroscopy

Attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy was applied for the first time to detect the structural changes upon photoreactions of redox cofactors in photosystem II (PSII). The PSII-enriched membranes from spinach were adsorbed on the surface of a silicon prism, and FTIR measurements of various redox cofactors were performed for the same sample but under different conditions by exchanging buffers in a flow cell. Light-induced FTIR difference spectra upon redox reactions of the oxygen-evolving Mn cluster, the primary quinone electron acceptor Q A, the redox-active tyrosine Y D, the primary electron acceptor pheophytin, and the primary electron donor chlorophyll P680 were successively recorded in buffers including different redox reagents and inhibitors. All of these cofactors remained active in the PSII membranes on the silicon surface, and the resultant spectra were basically identical to those previously recorded by the conventional transmission method. These ATR-FTIR measurements enable accurate comparison between reactions of different active sites in a single PSII sample. The present results demonstrated that the ATR-FTIR spectroscopy is a useful technique for investigation of the reaction mechanism of PSII.

Theoretical investigation of Q A −· -ligand interactions in bacterial reaction centers ofRhodobacter sphaeroides

Density functional theory was used to calculate magnetic resonance parameters for the primary stable electron acceptor anion radical (QA−·) in its binding site in the bacterial reaction center (bRC) ofRhodobacter sphaeroides. The models used for the calculations of the QA−· binding pocket included all short-range interactions of the ubiquinone with the protein surroundings in a gradual manner and thus allowed a decomposition and detailed analysis of the different specific interactions. Comparison of the obtained hyperfine and quadrupole couplings with experimental data demonstrates the feasibility and reliability of calculations on such complex biologically relevant systems. With these results, the interpretation of previously published 3-pulse electron spin echo envelope modulation data could be extended and an assignment of the observed double quantum peak to a specific amino acid is proposed. The computations provide evidence for a slightly altered binding site geometry for the QA ground state as investigated by X-ray crystallography with respect to the QAt-· anion radical state as accessible via EPR spectroscopy. This new geometry leads to improved fits of the W-band correlated-coupled radical pair spectra of QA−·-P865+· compared to orientation data from the crystal structure. Finally, a correlation of the14N quadrupole parameters of His219 with the hydrogen bond geometry and a comparison with previous systematic studies on the influence of hydrogen bond geometry on quadrupole coupling parameters (J. Fritscher: Phys. Chem. Chem. Phys. 6, 4950–4956, 2004) is presented.

Kinetics and mechanism of electron transfer in intact photosystem II and in the isolated reaction center: Pheophytin is the primary electron acceptor

The mechanism and kinetics of electron transfer in isolated D1/D2-cyt(b559) photosystem (PS) II reaction centers (RCs) and in intact PSII cores have been studied by femtosecond transient absorption and kinetic compartment modeling. For intact PSII, a component of approximately 1.5 ps reflects the dominant energy-trapping kinetics from the antenna by the RC. A 5.5-ps component reflects the apparent lifetime of primary charge separation, which is faster by a factor of 8-12 than assumed so far. The 35-ps component represents the apparent lifetime of formation of a secondary radical pair, and the approximately 200-ps component represents the electron transfer to the Q(A) acceptor. In isolated RCs, the apparent lifetimes of primary and secondary charge separation are approximately 3 and 11 ps, respectively. It is shown (i) that pheophytin is reduced in the first step, and (ii) that the rate constants of electron transfer in the RC are identical for PSII cores and for isolated RCs. We interpret the first electron transfer step as electron donation from the primary electron donor Chl(acc D1). Thus, this mechanism, suggested earlier for isolated RCs at cryogenic temperatures, is also operative in intact PSII cores and in isolated RCs at ambient temperature. The effective rate constant of primary electron transfer from the equilibrated RC* excited state is 170-180 ns(-1), and the rate constant of secondary electron transfer is 120-130 ns(-1).

A Protein Dynamics Study of Photosystem II: The Effects of Protein Conformation on Reaction Center Function

Molecular dynamics simulations have been performed to study photosystem II structure and function. Structural information obtained from simulations was combined with ab initio computations of chromophore excited states. In contrast to calculations based on the x-ray structure, the molecular-dynamics-based calculations accurately predicted the experimental absorbance spectrum. In addition, our calculations correctly assigned the energy levels of reaction-center (RC) chromophores, as well as the lowest-energy antenna chlorophyll. The primary and secondary quinone electron acceptors, Q A and Q B, exhibited independent changes in position over the duration of the simulation. Q B fluctuated between two binding sites similar to the proximal and distal sites previously observed in light- and dark-adapted RC from purple bacteria. Kinetic models were used to characterize the relative influence of chromophore geometry, site energies, and electron transport rates on RC efficiency. The fluctuating energy levels of antenna chromophores had a larger impact on quantum yield than did their relative positions. Variations in electron transport rates had the most significant effect and were sufficient to explain the experimentally observed multi-component decay of excitation in photosystem II. The implications of our results are discussed in the context of competing evolutionary selection pressures for RC structure and function.

Artificial Photosynthetic Reaction Centers with Carotenoid Antennas.

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Structure of the Hydrophilic Domain of Respiratory Complex I from Thermus thermophilus

Respiratory complex I plays a central role in cellular energy production in bacteria and mitochondria. Its dysfunction is implicated in many human neurodegenerative diseases, as well as in aging. The crystal structure of the hydrophilic domain (peripheral arm) of complex I from Thermus thermophilus has been solved at 3.3 angstrom resolution. This subcomplex consists of eight subunits and contains all the redox centers of the enzyme, including nine iron-sulfur clusters. The primary electron acceptor, flavin-mononucleotide, is within electron transfer distance of cluster N3, leading to the main redox pathway, and of the distal cluster N1a, a possible antioxidant. The structure reveals new aspects of the mechanism and evolution of the enzyme. The terminal cluster N2 is coordinated, uniquely, by two consecutive cysteines. The novel subunit Nqo15 has a similar fold to the mitochondrial iron chaperone frataxin, and it may be involved in iron-sulfur cluster regeneration in the complex.

Eficiência fotoquímica de gramíneas forrageiras tropicais submetidas à deficiência hídrica

Neste estudo, as espécies capim-setária (Setaria anceps Stapf.), capim-hemárthria (Hemarthria altissima [Poir] Stapf. & Hubbard), capim-do-nilo (Acroceras macrum Stapf.) e capim-angola (Brachiaria purpurascens [Raddi] Henr.) foram submetidos à deficiência hídrica moderada a seca com o objetivo de avaliar o efeito do déficit hídrico sobre as características de fluorescência da clorofila. O experimento foi realizado em casa de vegetação, em blocos ao acaso, constituídos pelas quatro espécies cultivadas sob dois regimes hídricos (irrigado e não-irrigado), em três repetições. Durante a indução da deficiência hídrica, foram monitoradas as seguintes variáveis de fluorescência da clorofila a: fluorescência inicial (F0), fluorescência máxima (Fm), rendimento quântico máximo do PSII (Fv/Fm), taxa relativa de transporte de elétrons (ETR), quenching fotoquímico (qP) e quenching não fotoquímico (qN). Após dez dias de submissão ao estresse hídrico, os valores de Fo e Fm decresceram em todas as espécies. Os menores valores de Fv/Fm foram encontrados no capim-do-nilo e no capim-setária, o que configura baixo rendimento fotoquímico nessas espécies sob déficit hídrico, ao contrário do capim-hemárthria, que apresentou valores similares em ambos os tratamentos. Os valores mais altos de qN foram registrados no capim-hemárthria e no capim-angola, demonstrando boa capacidade dessas espécies em dissipar a energia luminosa absorvida em excesso para manter baixo estado de redução nos aceptores primários de elétrons do PSII. Em geral, as curvas de ETR em resposta ao fluxo de fótons fotossintéticos mostraram-se distintas entre os tratamentos, sendo mais pronunciadas no capim-do-nilo. Nessa espécie, a eficiência dos transportadores de elétrons do PSII foi seriamente comprometida pelo déficit hídrico.

Selenite reduction by a denitrifying culture: batch- and packed-bed reactor studies

Selenite reduction by a bacterial consortium enriched from an oil refinery waste sludge was studied under denitrifying conditions using acetate as the electron donor. Fed-batch studies with nitrate as the primary electron acceptor showed that accumulation of nitrite led to a decrease in the extent of selenite reduction. Also, when nitrite was added as the primary electron acceptor, rapid selenite reduction was observed only after nitrite was significantly depleted from the medium. These results indicate that selenite reduction was inhibited at high nitrite concentrations. In addition to batch experiments, continuous-flow selenite reduction experiments were performed in packed-bed columns using immobilized enrichment cultures. These experiments were carried out in three phases: in phase I, a continuous nitrate feed with different inlet selenite concentration was applied; in phase II, nitrate was fed in a pulsed fashion; and in phase III, nitrate was fed in a continuous mode but at much lower concentrations than the other two phases. During the phase I experiments, little selenite was removed from the influent. However, when the column was operated in the pulse feed strategy (phase II) or in the continuous mode with low nitrate levels (phase III), significant quantities of selenium were removed from solution and retained in the immobilization matrix in the column. Thus, immobilized denitrifying cultures can be effective in removing selenium from waste streams, but nitrate-limited operating conditions might be required.

Global impact and application of the anaerobic ammonium-oxidizing (anammox) bacteria

In the anaerobic ammonium oxidation (anammox) process, ammonia is oxidized with nitrite as primary electron acceptor under strictly anoxic conditions. The reaction is catalysed by a specialized group of planctomycete-like bacteria. These anammox bacteria use a complex reaction mechanism involving hydrazine as an intermediate. The reactions are assumed to be carried out in a unique prokaryotic organelle, the anammoxosome. This organelle is surrounded by ladderane lipids, which make the organelle nearly impermeable to hydrazine and protons. The localization of the major anammox protein, hydrazine oxidoreductase, was determined via immunogold labelling to be inside the anammoxosome. The anammox bacteria have been detected in many marine and freshwater ecosystems and were estimated to contribute up to 50% of oceanic nitrogen loss. Furthermore, the anammox process is currently implemented in water treatment for the low-cost removal of ammonia from high-strength waste streams. Recent findings suggested that the anammox bacteria may also use organic acids to convert nitrate and nitrite into dinitrogen gas when ammonia is in short supply.

Inhibition of choline oxidase by quinoid dyes

Choline oxidase catalyzes the oxidation of choline to glycine-betaine, with betaine-aldehyde as intermediate and molecular oxygen as primary electron acceptor. This study reports on the inhibitory effects of triarylmethanes (cationic malachite green; neutral leukomalachite green), phenoxazines (cationic, meldola blue and nile blue; neutral nile red) and a structurally-related phenothiazine (methylene blue) on choline oxidase, assayed at 25°C in 50 mM MOPS buffer, pH 7, using choline as substrate. Methylene B acted as a competitive inhibitor with Ki = 74 ± 7.2 μM, pointing to the choline–binding site of the enzyme as a target site. Nile B caused noncompetitive inhibition of enzyme activity with Ki = 20 ± 4.5 μM. In contrast to methylene B and nile B, malachite G and meldola B caused complex, nonlinear inhibition of choline oxidase, with estimated Ki values in the micromolar range. The difference in kinetic pattern was ascribed to the differential ability of the dyes to interact (and interfere) with the flavin cofactor, generating different perturbations in the steady-state balance of the catalytic process.

Ultrafast Transient Absorption Studies on Photosystem I Reaction Centers from Chlamydomonas reinhardtii. 2: Mutations near the P700 Reaction Center Chlorophylls Provide New Insight into the Nature of the Primary Electron Donor

The energy transfer and charge separation kinetics in several core Photosystem I particles of Chlamydomonas reinhardtii with point mutations around the P A and P B reaction center chlorophylls (Chls) have been studied using ultrafast transient absorption spectroscopy in the femtosecond to nanosecond time range to characterize the influence on the early electron transfer processes. The data have been analyzed in terms of kinetic compartment models. The adequate description of the transient absorption kinetics requires three different radical pairs in the time range up to ∼100 ps. Also a charge recombination process from the first radical pair back to the excited state is present in all the mutants, as already shown previously for the wild-type (Müller, M. G., J. Niklas, W. Lubitz, and A. R. Holzwarth. 2003. Biophys. J. 85:3899–3922; and Holzwarth, A. R., M. G. Müller, J. Niklas, and W. Lubitz. 2005. J. Phys. Chem. B. 109:5903–59115). In all mutants, the primary charge separation occurs with the same effective rate constant within the error limits as in the wild-type (»350 ns −1), which implies an intrinsic rate constant of charge separation of <1 ps −1. The rate constant of the secondary electron transfer process is slowed down by a factor of ∼2 in the mutant B-H656C, which lacks the ligand to the central metal of Chl P B. For the mutant A-T739V, which breaks the hydrogen bond to the keto carbonyl of Chl P A, only a slight slowing down of the secondary electron transfer is observed. Finally for mutant A-W679A, which has the Trp near the P A Chl replaced, either no pronounced effect or, at best, a slight increase on the secondary electron transfer rate constants is observed. The effective charge recombination rate constant is modified in all mutants to some extent, with the strongest effect observed in mutant B-H656C. Our data strongly suggest that the Chls of the P A and P B pair, constituting what is traditionally called the “primary electron donor P700”, are not oxidized in the first electron transfer process, but rather only in the secondary electron transfer step. We thus propose a new electron transfer mechanism for Photosystem I where the accessory Chl(s) function as the primary electron donor(s) and the A 0 Chl(s) are the primary electron acceptor(s). This new mechanism also resolves in a straightforward manner the difficulty with the previous mechanism, where an electron would have to overcome a distance of ∼14 Å in <1 ps in a single step. If interpreted within a scheme of single-sided electron transfer, our data suggest that the B-branch is the active branch, although parallel A-branch activity cannot be excluded. All the mutations do affect to a varying extent the energy difference between the reaction center excited state RC* and the first radical pair and thus affect the rate constant of charge recombination. It is interesting to note that the new mechanism proposed is in fact analogous to the electron transfer mechanism in Photosystem II, where the accessory Chl also plays the role of the primary electron donor, rather than the special Chl pair P680 (Prokhorenko, V. and A. R. Holzwarth. 2000. J. Phys. Chem. B. 104:11563–11578).

Artificial photosynthetic reaction centers with carotenoid antennas

Two reaction center-antenna models based on a purpurin macrocycle linked to a C 60 and to a carotenoid polyene have been synthesized. In these systems the C 60 moiety is the primary electron acceptor, the purpurin is the primary electron donor and the carotenoid moiety acts both as an antenna and secondary electron donor. Formation of the initial charge separated state, C–Pur + –C 60 − , following excitation with light absorbed by either the purpurin or C 60 takes place on the 10 ps time scale. The final charge separated state, C + –Pur–C 60 − , is formed in one of the compounds with a quantum yield of 32% based upon light absorbed by the carotenoid. In order to function as an antenna, the carotenoid pigment must be electronically coupled to the purpurin. The purpurin C ring provides an excellent framework for locating a carotenoid polyene in partial conjugation with the macrocycle, leading to a relatively strong electronic communication between the chromophores; functionalization of a meso position of the purpurin provides a site for the covalent attachment of C 60.

The nature of the photosystem II reaction centre in the chlorophyll d-containing prokaryote, Acaryochloris marina

Pigment-protein complexes enriched in photosystem II (PS II) have been isolated from the chlorophyll (Chl) d containing cyanobacterium, Acaryochloris marina. A small PS II-enriched particle, we call 'crude reaction centre', contained 20 Chl d, 0.5 Chl a and 1 redox active cytochrome b-559 per 2 pheophytin a, plus the D1 and D2 proteins. A larger PS II-enriched particle, we call 'core', additionally bound the antenna complexes, CP47 and CP43, and had a higher chlorophyll per pheophytin ratio. Pheophytin a could be photoreduced in the presence of a strong reductant, indicating that it is the primary electron acceptor in photosystem II of A. marina. A substoichiometric amount of Chl a (less than one chlorophyll a per 2 pheophytin a) strongly suggests that Chl a does not have an essential role in the photochemistry of PS II in this organism. We conclude that PS II, in A. marina, utilizes Chl d and not Chl a as primary electron donor and that the primary electron acceptor is one of two molecules of pheophytin a.

Supramolecular triads bearing porphyrin and fullerene via ‘two-point’ binding involving coordination and hydrogen bonding

Supramolecular triads composed of fullerene (C 60) as primary electron acceptor, zinc porphyrin (ZnP) as primary electron donor, and either a ferrocene (Fc), or N, N-dimethylaminophenyl (DMA), or N, N-diphenylaminophenyl (DPA) entity as a second electron donor were constructed via a ‘two-point’ binding motif involving axial coordination and hydrogen bonding. The B3LYP/3-21G(*) optimized structures revealed disposition of the three entities of the triads in a triangular fashion. The redox behavior of the different components was studied using cyclic voltammetry in o-dichlorobenzene containing 0.1 M ( n-C 4H 9) 4NClO 4. The oxidation potentials of the second electron donor followed the trend: Fc<DMA<DPA, and the free-energy calculations suggested the possibility of the occurrence of sequential hole transfer in these triads. Efficient electron transfer from the excited singlet state of zinc porphyrin to the fullerene entity was observed in all of the studied triads in o-dichlorobenzene. Longer charge-separated states were observed for zinc porphyrin with a carboxylic acid compared with that having an amide group. The ratios of the experimentally determined forward to reverse electron transfer rates, k CS/ k CR were evaluated to be 10 3 for triads formed by zinc porphyrin with a carboxylic acid, suggesting charge stabilization in these triads.