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PubMed1998

Role of Arg180 of the D2 protein in photosystem II structure and function.

On the basis of sequence comparison with the M subunit of the reaction center of purple bacteria, no residues in photosystem II can be clearly identified that may be predicted to correspond to the His residue that binds one of the accessory bacteriochlorophylls in the purple bacterial reaction center. However, the Arg180 residue of the D2 protein is close to where this residue is predicted to be and could conceivably serve as a chlorophyll ligand. To analyze the function of Arg180, it was changed to nine different amino acids in the cyanobacterium Synechocystis sp. PCC 6803. Except for the Arg180-->Gln (R180Q) mutant, the resulting strains were no longer photoautotrophic. The properties of photosystem II upon mutation of Arg180 were probed in strains from which photosystem I had been deleted genetically. Mutations at the Arg180 residue affected oxygen evolution capacity and the amount of photosystem II that was present in thylakoids. Surprisingly, in the Arg180 mutants, EPR signals that may originate from the oxidized redoxactive Tyr160 of the D2 protein (Y(D)ox) were small and generally did not resemble the usual signal IIs, signifying an effect of the Arg180 mutations on the environment surrounding Tyr160. In addition, in most mutants, the charge recombination kinetics between the primary electron-accepting quinone in photosystem II (Q(A)-) and oxidized species on the donor side were faster upon introducing mutations at Arg180 suggesting an increased steady-state concentration of P680+ in the mutants. However, Arg180 mutations also affected Q(A)- oxidation by the secondary electron-accepting quinone (Q(B)). HPLC analysis showed that, in the Arg180 mutants that were assayed, the pheophytin/chlorophyll ratio of photosystem II had not changed, indicating that the mutations did not lead to a pheophytinization of one of the chlorophyll molecules. Even though the results presented do not provide positive evidence that Arg180 of the D2 protein corresponds in function to the ligand to the central Mg in an accessory bacteriochlorophyll in reaction centers of purple bacteria, it is clear that changes in Arg180 greatly affect Tyr160 and P680. Various scenarios are discussed that are compatible with the data presented, and include an apparently close interaction between Arg180, His189, and Tyr160, and the possibility of the involvement of multiple chlorophylls to together form P680.

Arginine↗

PubMed2003

Photosynthesis of overwintering evergreen plants.

In this review we focus on photosynthetic behavior of overwintering evergreens with an emphasis on both the acclimative responses of photosynthesis to cold and the winter behavior of photosynthesis in conifers. Photosynthetic acclimation is discussed in terms of the requirement for a balance between the energy absorbed through largely temperature-insensitive photochemical processes and the energy used for temperature-sensitive biochemical processes and growth. Cold acclimation transforms the xanthophyll-mediated nonphotochemical antenna quenching of absorbed light from a short-term dynamic response to a long-term sustained quenching for the whole winter period. This acclimative response helps protect the evergreen foliage from photooxidative damage during the winter when photosynthesis is restricted or prevented by low temperatures. Although the molecular mechanisms behind the sustained winter excitation quenching are largely unknown, it does involve major alterations in the organization and composition of the photosystem II antenna. In addition, photosystem I may play an important role in overwintering evergreens not only by quenching absorbed light photochemically via its support of cyclic electron transport at low temperatures, but also by nonphotochemical quenching of absorbed light irrespective of temperature. The possible role of photosystem II reaction centers in nonphotochemical quenching of absorbed energy in overwintering evergreens is also discussed. Processes like chlororespiration and cyclic electron transport may also be important for maintaining the functional integrity of the photosynthetic apparatus of overwintering evergreens both during periods of thawing in winter and during recovery from winter stress in spring. We suggest that the photosynthetic acclimation responses of overwintering evergreens represent specific evolutionary adaptations for plant species that invest in the long-term maintenance of leaf structure in cold climatic zones as exemplified by the boreal forests of the Northern Hemisphere.

Acclimatization↗

PubMed1991

Proline enhances primary photochemical activities in isolated thylakoid membranes of Brassica juncea by arresting photoinhibitory damage.

The presence of L-proline in the reaction mixture enhances the photosystem II (H2O----DCPIP) and whole chain (H2O----MV) catalysed electron transport activities of thylakoids isolated from the cotyledonary leaves of Brassica juncea seedlings raised in the absence and the presence of NaCl. The extent of stimulation in activities was higher in the thylakoids of NaCl raised plants than the controls. The extent of proline mediated stimulation was seen even in the presence of uncoupler NH4Cl suggesting that this stimulation is not due to uncoupling. However, photosystem I (DCPIPH2----MV) catalysed photoreaction remained almost insensitive to proline. The presence of proline in the incubation medium brought about a significant reduction in the time dependent loss in photochemical activity of thylakoids exposed to strong light suggesting that proline prevents photoinhibitory loss in chloroplast activity. Also, proline brought about a considerable reduction in the production of lipid peroxidation linked maiondialdehyde during strong illumination. We suggest that proline protects the components involved in water oxidation capacity by reducing the production of free radicals and/or scavenging the free radicals and thereby reducing thylakoid lipid peroxidation.

Ammonium Chloride↗

PubMed1991

Photosynthetic electron transport controls nitrogen assimilation in cyanobacteria by means of posttranslational modification of the glnB gene product.

A glnB gene is identified in the cyanobacterium Synechococcus sp. PCC 7942, and its gene product is found to be covalently modified as a result of imbalance in electron transfer in photosynthesis, where photosystem II is favored over photosystem I. The gene was cloned and sequenced and found to encode a polypeptide of 112 amino acid residues, whose sequence shows a high degree of similarity to the Escherichia coli regulatory protein, PII. In E. coli, PII is involved in signal transduction in transcriptional and post-translational regulation of nitrogen assimilation. Increase in ammonium ion concentration is shown to decrease covalent modification of the Synechococcus PII protein, as in enteric bacteria. We therefore propose that the photosynthetic electron transport chain may regulate the pathway of nitrogen assimilation in cyanobacteria by means of posttranslational, covalent modification of the glnB gene product. The existence of the glnB gene in different strains of cyanobacteria is demonstrated and its implications are discussed.

Amino Acid Sequence↗

PubMed2000

Electron flow between photosystem II and oxygen in chloroplasts of photosystem I-deficient algae is mediated by a quinol oxidase involved in chlororespiration.

In Chlamydomonas reinhardtii mutants deficient in photosystem I because of inactivation of the chloroplast genes psaA or psaB, oxygen evolution from photosystem II occurs at significant rates and is coupled to a stimulation of oxygen uptake. Both activities can be simultaneously monitored by continuous mass spectrometry in the presence of (18)O(2). The light-driven O(2) exchange was shown to involve the plastoquinone pool as an electron carrier, but not cytochrome b(6)f. Photosystem II-dependent O(2) production and O(2) uptake were observed in isolated chloroplast fractions. Photosystem II-dependent oxygen exchange was insensitive to a variety of inhibitors (azide, carbon monoxide, cyanide, antimycin A, and salicylhydroxamic acid) and radical scavengers. It was, however, sensitive to propyl gallate. From inhibitors effects and electronic requirements of the O(2) uptake process, we conclude that an oxidase catalyzing oxidation of plastoquinol and reduction of oxygen to water is present in thylakoid membranes. From the sensitivity of flash-induced O(2) exchange to propyl gallate, we conclude that this oxidase is involved in chlororespiration. Clues to the identity of the protein implied in this process are given by pharmacological and immunological similarities with a protein (IMMUTANS) identified in Arabidopsis chloroplasts.

Animals↗

PubMed1987

Interaction of photosystem I-derived protons with the water-splitting enzyme complex. Evidence for localized domains.

The induction of millisecond delayed fluorescence mediated by PS I-dependent proton pumping has been used as an indicator of the time course with which those protons equilibrate with sites on the oxygen-evolving enzyme complex (Bowes, J. M., and Crofts, A. R. (1978). Z. Naturforsch. 33C, 271-275). We found that the induction curves were retarded by a reversible exposure of non-energized thylakoids to low concentrations of the uncoupler, desaspidin, at alkaline, but not at neutral, pH. The induction curves were not retarded by increasing the buffering capacity of the thylakoid lumen with Tricine, and were inhibited by the energy transfer inhibitors, dicyclohexylcarbodiimide (DCCD) and triphenyltin chloride (TPT). These data suggest that the catalytic site of the water-splitting complex is located in proton-sequestering membrane domains, rather than at the lumen-exposed inner membrane surface, protons released during PS I-mediated electron transport might equilibrate with protonatable sites on the oxygen-evolving complex without passing through the lumen, and those protons may travel over specific conducting pathways which can be blocked by DCCD and TPT.

Chlorophyll↗

PubMed1981

Reaction center triplet states in photosystem I and photosystem II.

A photosystem I (PS I) particle has been prepared by lithium dodecyl sulfate digestion which lacks the acceptor X, and iron-sulfur centers B and A. Illumination of these particles at liquid helium temperature results in the appearance of a light-induced spin-polarized triplet signal observed by EPR. This signal is attributed to the triplet state of P-700, the primary donor, formed by recombination of the light induced radical pair P-700+ A1- (where A1 is the intermediate acceptor). Formation of the triplet does not occur if P-700 is oxidized or if A1 is reduced, prior to the illumination. A comparison of the P-700 triplet with that of P-680, the primary donor of Photosystem II, shows several differences. (1) The P-680 triplet is 1.5 mT (15 G) wider than the P-700 triplet. This is reflected by the zero-field splitting parameters, which indicate that P-700 is a slightly larger species than P-680. The zero-field splitting parameters do not indicate that either P-700 or P-680 are dimeric. (2) The P-700 triplet is induced by red and far-red light, while the P-680 triplet is induced only by red light. (3) The temperature dependences of the P-700 triplet and the P-680 triplet are different.

Chloroplasts↗

PubMed2003

Effects of extracellular pH on the metabolic pathways in sulfur-deprived, H2-producing Chlamydomonas reinhardtii cultures.

Sustained photoproduction of H(2) by the green alga, Chlamydomonas reinhardtii, can be obtained by incubating cells in sulfur-deprived medium [Ghirardi et al. (2000b) Trends Biotechnol. 18: 506; Melis et al. (2000) Plant Physiol. 122: 127]. The current work focuses on (a) the effects of different initial extracellular pHs on the inactivation of photosystem II (PSII) and O(2)-sensitive H(2)-production activity in sulfur-deprived algal cells and (b) the relationships among H(2)-production, photosynthetic, aerobic and anaerobic metabolisms under different pH regimens. The maximum rate and yield of H(2) production occur when the pH at the start of the sulfur deprivation period is 7.7 and decrease when the initial pH is lowered to 6.5 or increased to 8.2. The pH profile of hydrogen photoproduction correlates with that of the residual PSII activity (optimum pH 7.3-7.9), but not with the pH profiles of photosynthetic electron transport through photosystem I or of starch and protein degradation. In vitro hydrogenase activity over this pH range is much higher than the actual in situ rates of H(2) production, indicating that hydrogenase activity per se is not limiting. Starch and protein catabolisms generate formate, acetate and ethanol; contribute some reductant for H(2) photoproduction, as indicated by 3-(3,4-dichlorophenyl)-1,1-dimethylurea and 2,5-dibromo-6-isopropyl-3-methyl-1,4-benzoquinone inhibition results; and are the primary sources of reductant for respiratory processes that remove photosynthetically generated O(2). Carbon balances demonstrate that alternative metabolic pathways predominate at different pHs, and these depend on whether residual photosynthetic activity is present or not.

Aerobiosis↗

PubMed2002

Action spectrum of psbA gene transcription is similar to that of photoinhibition in Synechocystis sp. PCC 6803.

The photosystem II (PSII) reaction center protein D1 undergoes rapid light-dependent turnover, which is caused by photoinhibition. To identify the photoreceptor(s) involved in the light-dependent expression of the psbA gene encoding the D1 protein, we determined the action spectra of psbA transcription, PSII activity, photosynthesis and photoinhibition in Synechocystis sp. PCC 6803. In accordance with its phycobilisome antenna, PSII showed the highest activity in the spectral region from yellow to red and only low activity in the ultraviolet-A (UV-A) to green region. Photoinhibition, in turn, was fastest in UV-A to violet light and a minor peak was found in the orange region. The action spectrum of psbA transcription resembled closely that of photoinhibition, suggesting that photoinhibition creates a signal for up-regulation of the psbA gene.

Cyanobacteria↗

PubMedDate not supplied

Effect of membrane fluidity on photoinhibition of isolated thylakoids membranes at room and low temperature.

The relationship between thylakoid membrane fluidity and the process of photoinhibition at room and low (4 degrees C) temperature was investigated. Two different membrane perturbing agents--cholesterol and benzylalcohol were applied to manipulate the fluidity of isolated pea thylakoids. The photochemical activity of photosystem I (PSI) and photosystem II (PSII), polarographically determined, were measured at high light intensity for different time of illumination at both temperatures. The exposure of cholesterol- and benzylalcohol-treated thylakoid membranes to high light intensities resulted in inhibition of both studied photochemical activities, being more pronounced for PSII compared to PSI. Time dependencies of inhibition of PSI and PSII electron transport rates for untreated and membranes with altered fluidity were determined at 20 degrees C and 4 degrees C. The effect is more pronounced for PSII activity during low-temperature photoinhibition. The data are discussed in terms of the determining role of physico-chemical properties of thylakoid membranes for the response of photosynthetic apparatus to light stress.

Benzyl Alcohol↗

PubMed1990

Photoreduction of NADP+ by isolated reaction centers of photosystem II: requirement for plastocyanin.

The carrier of photosynthetically generated reducing power is the iron-sulfur protein ferredoxin, which provides directly, or via NADP+, reducing equivalents needed for CO2 assimilation and other metabolic reactions in the cell. It is now widely held that, in oxygenic photosynthesis, the generation of reduced ferredoxin-NADP+ requires the collaboration in series of two photosystems: photosystem II (PSII), which energizes electrons to an intermediate reducing potential and transfers them to photosystem I (PSI), which in turn is solely competent to energize electrons to the strong reducing potential required for the reduction of ferredoxin-NADP+ (the Z scheme). This investigation tested the premise of an alternative scheme, which envisions that PSII, without the involvement of PSI, is also capable of photoreducing ferredoxin-NADP+. We report here unexpected findings consistent with the alternative scheme. Isolated PSII reaction centers (completely free of PSI components), when supplemented with ferredoxin, ferredoxin-NADP+ oxidoreductase, and a PSII electron donor,1,5-diphenylcarbazide, gave a significant photoreduction of NADP+. A striking feature of this electron transfer from a PSII donor to the perceived terminal acceptor of PSI was its total dependence on catalytic quantities of plastocyanin, a copper-containing electron-transport protein hitherto known only as an electron donor to PSI.

Chlorophyll↗

PubMed1989

Interference of electron transport inhibitors with desaturation of monogalactosyl diacylglycerol in intact chloroplasts.

Isolated intact chloroplasts are able to desaturate fatty acids in newly synthesized monogalactosyl diacylglycerol. By analogy with other systems, this desaturation might be expected to involve electron carriers. The effects of electron transport inhibitors on chloroplast lipid-linked desaturation were therefore investigated. Because desaturation occurs in the dark and is not inhibited by compounds specifically blocking photosystem II, it appeared that the photosystems themselves did not participate. Several compounds that prevent enzymatic reoxidation of plastoquinol in thylakoid membranes at the Qz site or withdraw electrons from this lipophilic electron carrier inhibited desaturation in the dark. This inhibition could not be reversed by adding chemicals that donate electrons to photosystem I, indicating that carriers past the cytochrome b/f complex were not involved. Inhibitors of cyclic electron transport interfered with desaturation only at rather high concentrations or not at all. Additional compounds that block the reduction of quinones were slightly inhibitory. Dithioerythritol and KCN also inhibited desaturation, although their exact mode of action is unknown. Dinitrophenyl-iodonitrothymol (DNP-INT), stigmatellin, and myxothiazol did not block desaturation at concentrations that inhibited photosynthetic electron flow through the Qz site very efficiently. Therefore, these results argue against an involvement of the Qz site in desaturation. Accordingly, the inhibition by the other compounds seemingly interfering at the same site as well as that by electron acceptors could be due to interference at a different redox step in desaturation. In vitro these compounds function also as electron acceptors in diaphorase reactions catalyzed by ferredoxin:NADP oxidoreductase.

Acylation↗

PubMed2000

Revealing the structure of the photosystem II chlorophyll binding proteins, CP43 and CP47.

A review of the structural properties of the photosystem II chlorophyll binding proteins, CP47 and CP43, is given and a model of the transmembrane helical domains of CP47 has been constructed. The model is based on (i) the amino acid sequence of the spinach protein, (ii) an 8 A three-dimensional electron density map derived from electron crystallography and (iii) the structural homology which the membrane spanning region of CP47 shares with the six N-terminal transmembrane helices of the PsaA/PsaB proteins of photosystem I. Particular emphasis has been placed on the position of chlorophyll molecules assigned in the 8 A three-dimensional map of CP47 (K.-H. Rhee, E.P. Morris, J. Barber, W. Kühlbrandt, Nature 396 (1998) 283-286) relative to histidine residues located in the transmembrane regions of this protein which are likely to form axial ligands for chlorophyll binding. Of the 14 densities assigned to chlorophyll, the model predicted that five have their magnesium ions within 4 A of the imidazole nitrogens of histidine residues. For the remaining seven histidine residues the densities attributed to chlorophylls were within 4-8 A of the imidazole nitrogens and thus too far apart for direct ligation with the magnesium ion within the tetrapyrrole head group. Improved structural resolution and reconsiderations of the orientation of the porphyrin rings will allow further refinement of the model.

Amino Acid Sequence↗

PubMed1986

Differential detergent-solubilization of integral thylakoid membrane complexes in spinach chloroplasts. Localization of photosystem II, cytochrome b6-f complex and photosystem I.

Progressive solubilization of spinach chloroplast thylakoids by Triton X-100 was employed to investigate the domain organization of the electron transport complexes in the thylakoid membrane. Triton/chlorophyll ratios of 1:1 were sufficient to disrupt fully the continuity of the thylakoid membrane network, but not sufficient to solubilize either photosystem I (PSI), photosystem II (PSII) or the cytochrome b6-f(Cyt b6-f) complex. Progressive with the Triton concentration increase (Triton/Chl greater than 1:1), a differential solubilization of the three electron transport complexes was observed. Solubilization of the Cyt b6-f complex from the thylakoid membrane preceded that of PSI and apparently occurred early in the solubilization of stroma-exposed segments of the chloroplast lamellae. The initial removal of chlorophyll (up to 40% of the total) occurred upon solubilization of PSI from the stroma-exposed lamella regions in which PSI is localized. The tightly appressed membrane of the grana partition regions was markedly resistant to solubilization by Triton X-100. Thus, solubilization of PSII from this membrane region was initiated only after all Cyt b6-f and PSI complexes were removed from the chloroplast lamellae. The results support the notion of extreme lateral heterogeneity in the organization of the electron transport complexes in higher plant chloroplasts and suggest a Cyt b6-f localization in the membrane of the narrow fret regions which serve as a continuum between the grana and stroma lamellae.

Binding Sites↗

PubMed1985

Interactions between thylakoid electron transfer complexes. II. Modification studies with glutaraldehyde.

Photosystem I (PSI) and photosystem II (PSII) complexes have been isolated from stacked spinach thylakoid membranes that had been treated with varying amounts of glutaraldehyde. The concentrations of cytochrome f, Q, and P700 have been determined by spectrophotometric methods. It was found that at low concentrations of glutaraldehyde, the amount of cytochrome f associated with either PSII or PSI increased significantly while the amounts of Q and P700 stayed relatively constant. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblotting analyses indicated the presence of cytochrome f and other components of the cytochrome b6-f complex in the PSII and PSI preparations after glutaraldehyde treatment, but no intermolecular cross-linked polypeptides could be detected. Solubilization of the cytochrome b6-f complex was also inhibited after thylakoid membranes were treated with low concentrations of glutaraldehyde. These results are discussed in relation to current models for the organization of the membrane complexes, and relate to the location of the cytochrome b6-f complex in appressed and nonappressed membrane regions of thylakoids.

Aldehydes↗

PubMed1994

Mutation of chlorophyll ligands in the chlorophyll-binding CP47 protein as studied in a Synechocystis sp. PCC 6803 photosystem I-less background.

Site-directed mutations have been introduced to replace conserved histidine residues in the chlorophyll-binding protein CP47 of photosystem II (PS II) in a PS I-less/apcE-background strain of the cyanobacterium Synechocystis sp. PCC 6803. In thylakoids isolated from such a system, the degree of loss of the 695-nm fluorescence emission maximum at 77 K compared to that at 685 nm generally was consistent with the decrease in oxygen evolution rates measured at saturating light intensity. Taking into account that in the absence of CP47 and PS I some chlorophyll remains detectable in cells, the relative 695-nm fluorescence emission and the rate of oxygen evolution also correlate with the relative amount of chlorophyll per cell and with the number of PS II reaction centers on a chlorophyll basis. Interestingly, the 77 K fluorescence excitation spectra monitoring 695-nm emission of thylakoids from the CP47 His-to-Tyr mutants in a photosystem I-less/apcE-background showed increases in the 413- and 531-nm absorption regions, compared to spectra of thylakoids from the background strain. These wavelengths coincide with absorption maxima of pheophytin. No increase in the 531-nm excitation band was observed in thylakoids from mutants lacking PS II or with a His-to-Asn mutation. These results are interpreted to indicate that replacement of conserved histidine residues by tyrosine in CP47 leads to the loss of Mg2+ from chlorophyll, resulting in the formation of pheophytin, or to the binding of pheophytin (rather than chlorophyll) at a particular pigment-binding site of CP47 during biogenesis and assembly of the protein. It was observed that the light-harvesting efficiency of CP47 His mutants was lower judging from the light intensity dependence of electron transport and analysis of fluorescence decay kinetics. This suggests that the presence of pheophytin in the antenna decreases antenna efficiency.

Chlorophyll↗

PubMed1994

Differential transcription of plastome-encoded genes in the mesophyll and bundle-sheath chloroplasts of the monocotyledonous NADP-malic enzyme-type C4 plants maize and Sorghum.

The transcription of plastome-encoded genes in mesophyll and bundle-sheath chloroplasts of the monocotyledonous NADP-malic enzyme-type C4 species Zea mays L. (maize) and Sorghum bicolor (L.) Moench. was investigated. RNA accumulation and transcription were assayed starting from isolated mesophyll and bundle-sheath chloroplasts and using quantitative northern and run-on transcription analysis. Determination of the mesophyll to bundle-sheath ratios of transcript abundance in maize and Sorghum chloroplasts showed that the mRNAs of the plastome-encoded photosystem II genes analysed (psbA, psbB, psbD, psbH and psbE/F) varied from 2.5- to 4.0-fold (maize) and 3.1- to 5.2-fold (Sorghum), respectively. The rbcL transcript, in contrast, was more abundant in bundle-sheath chloroplasts of both species, about 3-fold in maize and more than 10-fold in Sorghum. On the other hand, transcripts of genes encoding the 16S ribosomal RNA (r16) and subunits of photosystem I (psaA) and the cytochrome b/f complex (petB, petA) accumulated to similar levels in both types of chloroplasts. Determination of absolute transcript levels for rbcL and psbA in chloroplasts from maize and Sorghum demonstrated that for both genes, the mesophyll to bundle-sheath differences in transcript abundance were more pronounced in Sorghum. Measurements of the transcriptional activities of rbcL and psbA showed that the transcription rate of rbcL is higher in bundle-sheath chloroplasts while psbA is more actively transcribed in mesophyll chloroplasts. The differences in the transcription rates between the two chloroplast types were again more pronounced in Sorghum, thus reflecting the differences between maize and Sorghum in the relative levels of the rbcL and psbA transcripts. However, although transcription rate and mRNA abundance are correlated, they did not exactly match one another. This indicates additional regulation of transcript abundance at the level of RNA stability.

Chloroplasts↗

PubMed2000

Picosecond time-resolved fluorescence studies on excitation energy transfer in a histidine 117 mutant of the D2 protein of photosystem II in Synechocystis 6803.

The role of the peripheral reaction center chlorophyll a molecule associated with His117 of the D2 polypeptide in photosystem II was investigated in Synechocystis sp. PCC 6803 using a combination of steady state, pump-probe, and picosecond time-resolved fluorescence spectroscopy. Data were obtained from intact cells and isolated thylakoid membranes of a control mutant and a D2-H117T mutant, both of which lacked photosystem I. Excitation energy transfer and trapping were investigated by analyzing the data with a kinetic model that used an exact numerical solution of the Pauli master equation, taking into account available photosystem II spectral and structural information. The results of our kinetic analysis revealed the observed difference in excited-state dynamics between the H117T mutant and the control to be consistent with a retardation of the rate of excitation energy transfer from the peripheral chlorophyll of D2 (Chl at His117) to the electron-transfer pigments and an increase of the rate constant for charge recombination in the H117T mutant. The kinetic model was able to account for the experimentally observed changes in absorption cross section and fluorescence decay kinetics between the control and mutant by invoking changes in only these two rate constants. The results rule out quenching of excitation by a chlorophyll cation radical as a mechanism responsible for the lower efficiency of excitation energy utilization in the H117T mutant. Our work also demonstrates the importance of the chlorophyll associated with His117 of the D2 protein for excitation energy transfer to the PSII electron-transfer pigments and for the effective stabilization of the primary radical pair.

Chlorophyll↗