chlorophyll-a and quinone

The X-ray-derived Photosystem II (PS II) structure from the thermophilic cyanobacterium

Topics: Benzoquinones; Chlorophyll; Electron Transport; Electrons; Iron; Kinetics; Light; Oxygen; Photosystem II Protein Complex; Synechocystis

Ozone (O

Topics: Air Pollutants; Antioxidants; Araceae; Benzoquinones; Biodegradation, Environmental; Catechin; Chlorophyll; Lipid Peroxidation; Malondialdehyde; Oxidation-Reduction; Oxidative Stress; Ozone; Salicylic Acid

In cyanobacteria, Glu-244 and Tyr-246 of the Photosystem II (PS II) D1 protein are hydrogen bonded to two water molecules that are part of a hydrogen-bond network between the bicarbonate ligand to a non-heme iron and the cytosol. Ala substitutions were introduced in Synechocystis sp. PCC 6803 to investigate the roles of these residues and the hydrogen-bond network on electron transfer between the primary plastoquinone acceptor, Q

Topics: Benzoquinones; Bicarbonates; Binding Sites; Chlamydomonas reinhardtii; Chlorophyll; Cyanobacteria; Electron Transport; Hydrogen Bonding; Iron; Mutant Proteins; Oxygen; Photosystem II Protein Complex; Plastoquinone; Synechocystis

In senescent leaves, chlorophyll typically is broken down to colorless and essentially photo-inactive phyllobilanes, which are linear tetrapyrroles classified as "nonfluorescent" chlorophyll catabolites (NCCs) and dioxobilane-type NCCs (DNCCs). In homogenates of senescent leaves of the tropical evergreen Spathiphyllum wallisii, when left at room temperature and extracted with methanol, the major endogenous, naturally formed NCC was regio- and stereoselectively oxidized (in part) to a mixture of its 15-hydroxy and 15-methoxy derivative. In the absence of methanol in the extract, only the 15-OH-NCC was observed. The endogenous oxidation process depended upon molecular oxygen. It was inhibited by carbon monoxide, as well as by keeping the leaf homogenate and extract at low temperatures. The remarkable "oxidative activity" was inactivated by heating the homogenate for 10 min at 70 °C. Upon addition of a natural epimeric NCC (epiNCC) to the homogenate of senescent or green Sp. wallisii leaves at room temperature, the exogenous epiNCC was oxidized regio- and stereoselectively to 15-OH-epiNCC and 15-OMe-epiNCC. The identical two oxidized epiNCCs were also obtained as products of the oxidation of epiNCC with dicyanodichlorobenzoquinone (DDQ). Water elimination from 15-OH-epiNCC occurred readily and gave a known "yellow" chlorophyll catabolite (YCC). The endogenous oxidation process, described here, may represent the elusive natural path from the colorless NCCs to yellow and pink coloured phyllobilins, which were found in (extracts of) some senescent leaves.

Topics: Benzoquinones; Chlorophyll; Cyanides; Hydroxides; Lilium; Oxidation-Reduction; Plant Extracts; Plant Leaves; Solvents; Stereoisomerism; Temperature; Tetrapyrroles

Photoinduced electron transfer with the electron donor-acceptor linked system of zinc-5,10,15,20-tetraphenylporphyrin (ZnTPP) as donor and benzoquinone (BQ) as acceptor was designed to mimic the electron transfer process in photosynthetic reaction center. Within the framework of the bimolecular electron transfer mechanisms of scanning electrochemical microscopy (SECM), the fundamental features of photoinduced electron transfer were demonstrated by recording the feedback approach curves under different light wavelength, intensity, and concentration of BQ. Meanwhile, relevant theoretical study was employed to support our proposal. It demonstrated that SECM as a new platform could also provide crucial information for simple simulation of the electron transfer process in photosynthetic reaction center.

Topics: Benzoquinones; Chlorophyll; Coloring Agents; Electrodes; Electron Transport; Light; Photosynthesis; Porphyrins; Spectrophotometry, Ultraviolet; Thermodynamics; Tin Compounds; Zinc

Dissolved organic matter (DOM) has been shown to affect phytoplankton species directly. These interactions largely depend on the origin and molecular size of DOM and are different in prokaryotes and eukaryotes. In a preceding study, however, two humic substance preparations did not adversely affect coccal green algae or cyanobacterial growth even at high concentrations of dissolved organic carbon (DOC). These results contradicted previous findings, showing a clear, negative response of different phototrophs to much lower DOC concentrations. To test whether or not at least defined building blocks of humic substances (HSs) are effective algicidal structures, we enriched two humic preparations with hydroquinone and p-benzoquinone, respectively, and exposed two different green algae, Pseudokirchneriella subcapitata and Monoraphidium braunii, and two cyanobacterial species, Synechocystis sp. and Microcystis aeruginosa, to the unmodified and enriched HSs. As response variables, growth rates in terms of biomass increase, chlorophyll-a content, and photosynthetic yield were measured. The highest concentration (4.17 mM DOC) of the modified HSs clearly inhibited growth; the cyanobacterial species were much more sensitive than the green algal species. However, realistic ecological concentrations did not adversely affect growth. Aerating the exposure solution for 24 h strongly reduced the inhibitory effect of the modified HSs. The algicidal effect was obviously caused by monomers and not by polymerised high molecular weight HSs themselves. Furthermore, the maximum quantum yield (Φ PSII max) was stimulated in the green algal species by low and medium DOC concentrations, but reduced in the cyanobacterial species upon exposure to higher HS concentrations. The quinone- and phenol-enriched HSs only showed algicidal activity at high concentrations of 4.17 mM DOC and lost their effects over time, presumably by oxidation and subsequent polymerisation. This study confirms that the applied humic substances themselves are not effective algicides even if enriched in effective structures.

Topics: Benzoquinones; Biomass; Chlorophyll; Chlorophyll A; Chlorophyta; Cyanobacteria; Humic Substances; Hydroquinones; Phenol; Photosystem II Protein Complex; Quantum Theory

In a previous study, we measured the redox potential of the primary electron acceptor pheophytin (Phe) a of photosystem (PS) II in the chlorophyll d-dominated cyanobacterium Acaryochloris marina and a chlorophyll a-containing cyanobacterium, Synechocystis. We obtained the midpoint redox potential (E(m)) values of -478 mV for A. marina and -536 mV for Synechocystis. In this study, we measured the redox potentials of the primary electron acceptor quinone molecule (Q(A)), i.e., E(m)(Q(A)/Q(A)(-)), of PS II and the energy difference between [P680·Phe a(-)·Q(A)] and [P680·Phe a·Q(A)(-)], i.e., ΔG(PhQ). The E(m)(Q(A)/Q(A)(-)) of A. marina was determined to be +64 mV without the Mn cluster and was estimated to be -66 to -86 mV with a Mn-depletion shift (130-150 mV), as observed with other organisms. The E(m)(Phe a/Phe a(-)) in Synechocystis was measured to be -525 mV with the Mn cluster, which is consistent with our previous report. The Mn-depleted downshift of the potential was measured to be approximately -77 mV in Synechocystis, and this value was applied to A. marina (-478 mV); the E(m)(Phe a/Phe a(-)) was estimated to be approximately -401 mV. These values gave rise to a ΔG(PhQ) of -325 mV for A. marina and -383 mV for Synechocystis. In the two cyanobacteria, the energetics in PS II were conserved, even though the potentials of Q(A)(-) and Phe a(-) were relatively shifted depending on the special pair, indicating a common strategy for electron transfer in oxygenic photosynthetic organisms.

Topics: Benzoquinones; Chlorophyll; Chlorophyll A; Cyanobacteria; Electron Transport; Energy Metabolism; Oxidation-Reduction; Pheophytins; Photosystem II Protein Complex; Spinacia oleracea; Synechocystis

Natural polyisoprene is a biopolymer consisting of isoprene units (C(5)H(8)) that is used commercially in household, medical, and industrial materials. For the management of natural polyisoprene production, the selection of high-yield polyisoprene-producing trees, and an understanding of polyisoprene biosynthesis, a high-throughput and highly sensitive screening method for the quantification of polyisoprene is required. In this study, we examined pyrolysates from polyisoprenes, polyprenols, carotenoids, ubiquinone (CoQ-10), and sterols by pyrolysis gas chromatography/mass spectrometry (PyGC/MS) and determined that the amounts of isoprene and limonene released from polyprenols and polyisoprenes were dependent upon their molecular weights. Based on these results, we developed a relative quantification method for polyisoprene in leaves by direct analysis of 1 mg of leaves using PyGC/MS. This novel quantification method eliminated extraction steps and can be used in the measurement of polyisoprene contents in Eucommia ulmoides and Hevea brasiliensis.

Topics: Benzoquinones; Butadienes; Carotenoids; Chlorophyll; Cyclohexenes; Eucommiaceae; Gas Chromatography-Mass Spectrometry; Hemiterpenes; Hevea; High-Throughput Screening Assays; Latex; Limonene; Molecular Weight; Pentanes; Sterols; Terpenes

Electron transport processes were investigated in barley leaves in which the oxygen-evolution was fully inhibited by a heat pulse (48 degrees C, 40 s). Under these circumstances, the K peak (approximately F(400 micros)) appears in the chl a fluorescence (OJIP) transient reflecting partial Q(A) reduction, which is due to a stable charge separation resulting from the donation of one electron by tyrozine Z. Following the K peak additional fluorescence increase (indicating Q(A)(-) accumulation) occurs in the 0.2-2 s time range. Using simultaneous chl a fluorescence and 820 nm transmission measurements it is demonstrated that this Q(A)(-) accumulation is due to naturally occurring alternative electron sources that donate electrons to the donor side of photosystem II. Chl a fluorescence data obtained with 5-ms light pulses (double flashes spaced 2.3-500 ms apart, and trains of several hundred flashes spaced by 100 or 200 ms) show that the electron donation occurs from a large pool with t(1/2) approximately 30 ms. This alternative electron donor is most probably ascorbate.

Topics: Benzoquinones; Biological Transport; Chlorophyll; Chlorophyll A; Darkness; Electron Transport; Fluorescence; Hordeum; Hot Temperature; Light; Oxidation-Reduction; Oxygen; Paraquat; Photosynthesis; Photosystem II Protein Complex; Plant Leaves; Plastocyanin; Tyrosine

The Qy absorption band of two chlorophyll derivatives, zinc chlorin e6 (ZnCe6) and zinc pheophorbide a (ZnPheida), in aqueous solution is bathochromically shifted on addition of quinones, e.g., 1,4-benzoquinone (BQ), with a corresponding shift of the fluorescence band. This is due to a complex formation of zinc chlorins induced by BQs and subsequent rearrangement. The time-resolved absorption spectra after laser pulse excitation show triplet quenching of the pigments by BQ and other quinones via electron transfer. The effects of electron transfer to noncovalently bound BQs were also studied with de novo synthesized peptides, into which ZnCe6 and ZnPheida were incorporated as model systems for the primary steps of photosynthetic reaction centers. Whereas the photophysical properties are similar to those of the unbound zinc chlorins, no BQ-mediated complex formation was observed.

Topics: Benzoquinones; Chlorophyll; Chlorophyllides; Kinetics; Organometallic Compounds; Porphyrins; Protein Conformation; Spectrometry, Fluorescence; Spectrophotometry, Ultraviolet; Zinc

The effect of oxygen concentration on both absorption and chlorophyll fluorescence spectra was investigated in isolated pea thylakoids at weak actinic light under the steady-state conditions. Upon the rise of oxygen concentration from anaerobiosis up to 412 microM a gradual absorbance increase around both 437 and 670 nm was observed, suggesting the disaggregation of LHCII and destacking of thylakoids. Simultaneously, an increase in oxygen concentration resulted in a decline in the Chl fluorescence at 680 nm to about 60% of the initial value. The plot of normalized Chl fluorescence quenching, F(-O(2))/F(+O(2)), showed discontinuity above 275 microM O(2), revealing two phases of quenching, at both lower and higher oxygen concentrations. The inhibition of photosystem II by DCMU or atrazine as well as that of cyt b(6)f by myxothiazol attenuated the oxygen-induced quenching events observed above 275 microM O(2), but did not modify the first phase of oxygen action. These data imply that the oxygen mediated Chl fluorescence quenching is partially independent on non-cyclic electron flow. The second phase of oxygen-induced decline in Chl fluorescence is diminished in thylakoids with poisoned PSII and cyt b(6)f activities and treated with rotenone or N-ethylmaleimide to inhibit NAD(P)H-plastoquinone dehydrogenase. The data suggest that under weak light and high oxygen concentration the Chl fluorescence quenching results from interactions between oxygen and PSI, cyt b(6)f and Ndh. On the contrary, inhibition of non-cyclic electron flow by antimycin A or uncoupling of thylakoids by carbonyl cyanide m-chlorophenyl hydrazone did not modify the steady-state oxygen effect on Chl fluorescence quenching. The addition of NADH protected thylakoids against oxygen-induced Chl fluorescence quenching, whereas in the presence of exogenic duroquinone the decrease in Chl fluorescence to one half of the initial level did not result from the oxygen effect, probably due to oxygen action as a weak electron acceptor from PQ pool and an insufficient non-photochemical quencher. The data indicate that mechanism of oxygen-induced Chl fluorescence quenching depends significantly on oxygen concentration and is related to both structural rearrangement of thylakoids and the direct oxygen reduction by photosynthetic complexes.

Topics: Absorption; Benzoquinones; Chlorophyll; Cytochromes; Fluorescence; NAD; Oxygen; Photosystem II Protein Complex; Pisum sativum; Spectrum Analysis; Thylakoids

Photosystems I and II (PSI and II) are reaction centres that capture light energy in order to drive oxygenic photosynthesis; however, they can only do so by interacting with the multisubunit cytochrome b(6)f complex. This complex receives electrons from PSII and passes them to PSI, pumping protons across the membrane and powering the Q-cycle. Unlike the mitochondrial and bacterial homologue cytochrome bc(1), cytochrome b(6)f can switch to a cyclic mode of electron transfer around PSI using an unknown pathway. Here we present the X-ray structure at 3.1 A of cytochrome b(6)f from the alga Chlamydomonas reinhardtii. The structure bears similarities to cytochrome bc(1) but also exhibits some unique features, such as binding chlorophyll, beta-carotene and an unexpected haem sharing a quinone site. This haem is atypical as it is covalently bound by one thioether linkage and has no axial amino acid ligand. This haem may be the missing link in oxygenic photosynthesis.

Topics: Animals; Benzoquinones; beta Carotene; Binding Sites; Chlamydomonas reinhardtii; Chlorophyll; Crystallography, X-Ray; Cytochrome b6f Complex; Dimerization; Heme; Ligands; Lipid Metabolism; Models, Molecular; Protein Structure, Quaternary; Protein Structure, Secondary

The oxidized primary electron donor in photosystem II, P(680)(+), is reduced in several phases, extending over 4 orders of magnitude in time. Especially the slower phases may reflect the back-pressure exerted by water oxidation and provide information on the reactions involved. The kinetics of secondary electron-transfer reactions in the microseconds time range after charge separation were investigated in oxygen-evolving thylakoids suspended in H2O or D2O. Flash-induced changes of chlorophyll fluorescence yield and electric field-induced recombination luminescence were decomposed into contributions from oxidation states S(0), S(1), S(2), and S(3) of the oxygen-evolving complex and interpreted in terms of stabilization kinetics of the initial charge-separated state S(j)Y(Z)P(680)(+)Q(A)(-)Q(B). In approximately 10% of the centers, only charge recombination took place. Otherwise, no static heterogeneity was involved in the microsecond reduction of P(680)(+) by Y(Z) (stabilization) or Q(A)(-) (recombination). The recombination component in active centers occurs mainly upon charge separation in S(3), and, in the presence of D2O, in S(2) as well and is tentatively attributed to the presence of Y(Z)(ox)S(j-1) in equilibrium with Y(Z)S(j). A 20-30 micros stabilization occurs in all S-states, but to different extents. Possible mechanisms for this component are discussed. D2O was found to decrease: (i) the rate of the reaction Y(Z)(ox)S(1) to Y(Z)S(2), (ii) the equilibrium constant between P680(+)Y(Z)S(2) and P(680)Y(Z)(ox)S(2), (iii) the rate of the slow phase of P(680)(+) reduction for the S(3) --> S(0) transition, and (iv) the rate of electron transfer from Q(A)(-) to Q(B) /Q(B)(-). The increased 'miss probability' in D2O is due to (iii).

Topics: Benzoquinones; Chlorophyll; Confidence Intervals; Deuterium Oxide; Electric Conductivity; Electron Transport; Kinetics; Lasers; Light-Harvesting Protein Complexes; Luminescent Measurements; Oxidation-Reduction; Photolysis; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Protons; Spectrometry, Fluorescence; Spinacia oleracea; Time Factors; Water

The 4 A structural model of photosystem I (PSI) has elucidated essential features of this protein complex. Inter alia, it demonstrates that the core proteins of PSI, PsaA and PsaB each consist of an N-terminal antenna-binding domain, and a C-terminal reaction center (RC)-domain. A comparison of the RC-domain of PSI and the photosynthetic RC of purple bacteria (PbRC), reveals significantly analogous structures. This provides the structural support for the hypothesis that the two RC-types (I and II) share a common evolutionary origin. Apart from a similar set of constituent cofactors of the electron transfer system, the analogous features include a comparable cofactor arrangement and a corresponding secondary structure motif of the RC-cores. Despite these analogies, significant differences are evident, particularly as regards the distances between and the orientation of individual cofactors, and the length and orientation of alpha-helices. Inferred roles of conserved amino acids are discussed for PSI, photosystem II (PSII), photosystem C (PSC, green sulfur bacteria) and photosystem H (PSH, heliobacteria). Significant sequence homology between the N-terminal, antenna-binding domains of the core proteins of type-I RCs, PsaA, PsaB, PscA and PshA (of PSI, PSC and PSH respectively) with the antenna-binding subunits CP43 and CP47 of PSII indicate that PSII has a modular structure comparable to that of PSI.

Topics: Amino Acid Sequence; Bacteria; Benzoquinones; Chlorophyll; Electron Transport; Iron; Models, Structural; Molecular Sequence Data; Oxygen; Photosynthetic Reaction Center Complex Proteins; Pyrroles; Sequence Homology, Amino Acid; Tetrapyrroles

Quinones caused quenching of Chl a fluorescence in native and model systems. Menadione quenched twofold the fluorescence of Chl a and BChl a in pea chloroplasts, chromatophores of purple bacteria, and liposomes at concentrations of 50-80 microM. To obtain twofold quenching in Triton X-100 micelles and in ethanol, the addition of 1.3 mM and 11 mM menadione was required, respectively. A proportional decrease in the lifetime and yield of Chl a fluorescence in chloroplasts, observed as the menadione concentration increased, is indicative of the efficient excitation energy transfer from bulk Chl to menadione. The decrease in the lifetime and yield of fluorescence was close to proportional in liposomes, but not in detergent micelles. The insensitivity of the menadione quenching effect to DCMU in chloroplasts, and similarity of its action in chloroplasts and liposomes indicate that menadione in chloroplasts interacts with antenna Chl, i.e., nonphotochemical quenching of fluorescence occurs.

Topics: Bacterial Chromatophores; Bacteriochlorophylls; Benzoquinones; Chlorophyll; Chlorophyll A; Chloroplasts; Diuron; Fluorescence; Liposomes; Micelles; Pisum sativum; Quinones; Rhodobacter sphaeroides; Rhodospirillum rubrum; Spectrometry, Fluorescence; Ubiquinone; Vitamin K

The pathway of proton transfer in the reaction center (RC) from Rhodobacter sphaeroides was investigated by site-directed mutagenesis. Ser-L223, a putative proton donor that forms a hydrogen bond with the secondary quinone acceptor QB, was replaced with Ala and Thr. RCs with Ala-L223 displayed reduced electron transfer and proton uptake rates in the reaction QA-QB- + 2H+----QAQBH2. The rate constant for this reaction, k(2)AB, was found to be reduced approximately 350-fold to 4.0 +/- 0.2 s-1. Proton uptake measurements using a pH indicator dye showed a rapid uptake of 1 H+ per RC followed by a slower uptake of 1 H+ per RC at a rate of 4.1 +/- 0.1 s-1; native RCs showed a rapid uptake of 2H+ per RC. Evidence is provided that these changes were not due to gross structural changes in the binding site of QB. RCs with Thr-L223 showed little reduction in the rates of electron and proton transfer. These results indicate that proton transfer from the hydroxyl group of Ser-L223 or Thr-L223 is required for fast electron and proton transfer associated with the formation of the dihydroquinone QH2. In contrast, previous work showed that replacing Glu-L212, another putative proton donor to QB, with Gln slowed proton uptake from solution without significantly altering electron transfer. We propose a model that involves two distinct proton transfer steps. The first step occurs prior to transfer of the second electron to QB and involves proton transfer from Ser-L223. The second step occurs after this electron transfer through a pathway involving Glu-L212.

Topics: Alanine; Benzoquinones; Chlorophyll; Electron Spin Resonance Spectroscopy; Electron Transport; Hydroquinones; Kinetics; Light-Harvesting Protein Complexes; Mutation; Oxidation-Reduction; Photosynthesis; Photosynthetic Reaction Center Complex Proteins; Plant Proteins; Protons; Quinones; Rhodobacter sphaeroides; Serine

The light-harvesting chlorophyll a/b complex (LHC II) and four photosystem II (PS II) core proteins (8.3, 32, 34 and 44 kDa) become phosphorylated in response to reduction of the intersystem electron transport chain of green plant chloroplasts. Previous studies indicated that reduction of the plastoquinone (PQ) pool is the key event in kinase activation. However, we show here that, unlike PS II proteins, LHC II is phosphorylated only when the cytochrome b6f complex is active. Two lines of evidence support this conclusion. (1) 2,5-Dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB) and the 2,4-dinitrophenyl ether of iodonitrothymol (DNP-INT), which are known to block electron flow into the cytochrome complex, selectively inhibit LHC II phosphorylation in spinach thylakoids. (2) The hcf6 mutant of maize, which contains PQ but lacks the cytochrome b6f complex, phosphorylates the four PS II proteins but fails to phosphorylate LHC II in vivo or in vitro.

Topics: Benzoquinones; Chlorophyll; Chloroplasts; Cytochrome b Group; Cytochrome b6f Complex; Cytochromes; Cytochromes f; Dinitrobenzenes; Hydroxyquinolines; Mutation; Phosphoproteins; Phosphorylation; Photosynthesis; Plants; Quinones

An O2-evolving photosystem II (PSII) reaction center complex was prepared from wheat by a simple method consisting of octylglucoside solubilization of Triton PSII particles followed by one-step sucrose density gradient centrifugation. The complex contained six species of proteins including the 33-kDa extrinsic protein with the same relative abundance as in the original PSII particles, one cytochrome b559, 4 Mn, and about 40 chlorophyll (Chl) per O2-evolving unit, and evolved O2 at a high rate of 1400-1700 mumol O2/mg Chl/h. O2 evolution by the complex was dependent on acceptor species, showing a hierarchy, ferricyanide greater than dichlorobenzoquinone greater than phenylbenzoquinone greater than dimethylbenzoquinone greater than duroquinone, and insensitive to DCMU, indicative of disjunction of the secondary quinone acceptor of PSII from the electron transport pathway. O2 evolution also showed a marked dependence on Cl- and Ca2+: about 10-fold acceleration by Cl- and an additional 2- to 3-fold by Ca2+. Comparison of the dissociation constants for Cl- and Ca2+ between the complex and NaCl-washed PSII particles revealed that octylglucoside treatment gives rise to a new Ca2+-sensitive site by removal of some unknown factor(s) other than the extrinsic 22- and 16-kDa proteins, while it preserves the Cl(-)-sensitive site as native as in NaCl-washed PSII particles. Analysis of the relationship between Cl- demand and Ca2+ demand revealed that Ca2+ absence noncompetitively inhibits the Cl(-)-supported O2 evolution, indicative of the independence of the binding site of these two factors.

Topics: Benzoquinones; Calcium; Chlorides; Chlorophyll; Cytochrome b Group; Diuron; Electron Transport; Hydrogen-Ion Concentration; Light-Harvesting Protein Complexes; Manganese; Oxidation-Reduction; Oxygen; Photosynthetic Reaction Center Complex Proteins; Photosystem II Protein Complex; Plant Proteins; Quinones; Solubility; Spectrometry, Fluorescence; Triticum

Topics: Benzoquinones; Carotenoids; Chlorophyll; Chloroplasts; Chromatography; Photosynthesis; Plants; Plants, Edible; Quinones; Research; Spectrum Analysis; Spinacia oleracea; Vitamin E; Vitamin K 1