jkruk@mol.uj.edu.pl Biochim Biophys Acta. 2019 Jan 28;12:18. doi: 10.1186/s13068-019-1355-5. It is a metallo-oxo cluster comprising four manganese ions (in oxidation states ranging from +2 to +4)[6] and one divalent calcium ion. The oxidation of water to molecular oxygen requires extraction of four electrons and four protons from two molecules of water. Kim EH, Lee DW, Lee KR, Jung SJ, Jeon JS, Kim HU.  |  Kurreck J, Seeliger AG, Reifarth F, Karge M, and Renger G (1995) Reconstitution of the Endogenous Plastoquinone Pool in Photosystem II (PS II) Membrane Fragments, Inside-Out-Vesicles, and PS II Core Complexes from Spinach. Plastoquinone (PLQ) acts as an electron carrier between photosystem II (PSII) and the cytochrome b6f complex. 2006;57(8):1677-84. doi: 10.1093/jxb/erl002. [12] Knowing the structure of Photosystem II did not suffice to reveal how it works exactly. Epub 2011 Dec 13. [8][9][10] While obtaining these structures was in itself a great feat, they did not show the oxygen-evolving complex in full detail.  |  Photosystem II (or water-plastoquinone oxidoreductase) is the first protein complex in the light-dependent reactions of oxygenic photosynthesis. Get the latest public health information from CDC: https://www.coronavirus.gov, Get the latest research information from NIH: https://www.nih.gov/coronavirus, Find NCBI SARS-CoV-2 literature, sequence, and clinical content: https://www.ncbi.nlm.nih.gov/sars-cov-2/. Epub 2011 Oct 18. Frederix1, Xavier Periole1 & Siewert J. Marrink1 Plastoquinone (PLQ) acts as an electron carrier between photosystem II (PSII) and the cytochrome b 6f complex. When it oxidizes water, producing oxygen gas and protons, it sequentially delivers the four electrons from water to a tyrosine (D1-Y161) sidechain and then to P680 itself. Please enable it to take advantage of the complete set of features! The most common form of plastoquinone, known as PQ-A or PQ-9, is a 2,3-dimethyl-1,4-benzoquinone molecule with a side chain of nine isoprenyl units. Biochim Biophys Acta. In relation to chlorophyll, after 18 h of growth under low light with the inhibitor, the content of alpha-tocopherol was 22.2 mol/1000 mol chlorophyll and that of total plastoquinone (oxidized and reduced) was 19 mol/1000 mol chlorophyll, while after 2 h of high-light stress the corresponding amounts dropped to 6.4 and 6.2 mol/1000 mol chlorophyll for alpha-tocopherol and total plastoquinone, respectively. Two functional sites of phosphatidylglycerol for regulation of reaction of plastoquinone Q(B) in photosystem II. In Photosystem II, the electron is then passed to a pheophytin molecule. Chem. Photosystem II (PSII), the light-driven water/plastoquinone photooxidoreductase, is of central importance in the planetary energy cycle. [7] Over the next years the resolution of the model was gradually increased to 2.9Å. Plastoquinol is more active than α-tocopherol in singlet oxygen scavenging during high light stress of Chlamydomonas reinhardtii. The calculated turnover rates under high-light conditions were twofold higher for total plastoquinone (0.23 nmol/h/ml of cell culture) than for alpha-tocopherol (0.11 nmol/h/ml). For example, subunit O is, Absorbs light energy and converts it to chemical energy, Mobile intra-thylakoid membrane electron carrier, Also known as the oxygen evolving center, or OEC, This page was last edited on 31 October 2020, at 01:02. The picture shows a top view of photosystem II (PDB entry 1s5l ), showing all of the light-absorbing molecules inside. 2012 Feb;1817(2):287-97. doi: 10.1016/j.bbabio.2011.10.002. eCollection 2019.  |  … The psbEFLJ operon of tobacco plastids encodes four bitopic low molecular mass transmembrane components of photosystem II. [19], First protein complex in light-dependent reactions of oxygenic photosynthesis, Photosynthetic reaction centre protein family, "Photosystem II: evolutionary perspectives", "Crystal structure of oxygen-evolving photosystem II from Thermosynechococcus vulcanus at 3.7-A resolution", "Architecture of the photosynthetic oxygen-evolving center", "Crystal structure of oxygen-evolving photosystem II at a resolution of 1.9 Å", "Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses", "Structure of photosystem II and substrate binding at room temperature", "Light-induced structural changes and the site of O=O bond formation in PSII caught by XFEL", "Evidence for intermediate S-states as initial phase in the process of oxygen-evolving complex oxidation", "Mechanism of light induced water splitting in Photosystem II of oxygen evolving photosynthetic organisms", Trans-acenaphthene-1,2-diol dehydrogenase, Photosynthetic reaction center complex proteins, Branched-chain alpha-keto acid dehydrogenase complex, Phosphoenolpyruvate sugar phosphotransferase system, https://en.wikipedia.org/w/index.php?title=Photosystem_II&oldid=986304870, Short description is different from Wikidata, Creative Commons Attribution-ShareAlike License, Reaction center protein, binds Chlorophyll P680, pheophytin, beta-carotene,quinone and manganese center, By convention, gene names are formed by Psb + subunit letter. Labeling patterns by azido-atrazine are compared for thylakoids, plastoquinone-depleted thylakoids, and different photosystem II preparations from spinach and Chlamydomonas. Comparative transcriptome analysis of a long-time span two-step culture process reveals a potential mechanism for astaxanthin and biomass hyper-accumulation in. This site needs JavaScript to work properly. In the photosystem II (PSII) of oxygenic photosynthetic organisms, the reaction center (RC) core mediates the light-induced electron transfer leading to water splitting and production of reduced plastoquinone molecules. DCMU in plastoquinone-depleted thylakoids can be displaced from the membrane by various substituted 1,4-benzoquinones, including plastoquinone-1. The S1 state is largely considered to consist of manganese ions with oxidation states of Mn3+, Mn3+, Mn4+, Mn4+. Abstract: Photosystem II (PSII) continuously attracts the attention of researchers aiming to unravel the riddle of its functioning and efficiency fundamental for … USA.gov. Plastoquinone (PQ) is an isoprenoid quinone molecule involved in the electron transport chain in the light-dependent reactions of photosynthesis. Singlet Oxygen Metabolism: From Genesis to Signaling. Within the photosystem, enzymes capture photons of light to energize electrons that are then transferred through a variety of coenzymes and cofactors to reduce plastoquinone to plastoquinol. Photosystem II: Structure and mechanism of the water:plastoquinone oxidoreductase By Jan Kern Kinetics of S 2 and S 3 Reduction by Tyrosine Y D and Other Endogenous Donors As a Function of Temperature in Spinach PS II Membrane Fragments with a Reconstituted Plastoquinone Pool † COVID-19 is an emerging, rapidly evolving situation. In the absence of light, the OEC will "relax" to the S1 state; the S1 state is often described as being "dark-stable". It has been found that in Chlamydomonas reinhardtii cells, under high-light stress, the level of reduced plastoquinone considerably increases while in the presence of pyrazolate, an inhibitor of plastoquinone and tocopherol biosynthesis, the content of reduced plastoquinone quickly decreases, similarly to alpha-tocopherol. eCollection 2017. While photosystem II (PSII) of plants utilizes light for photosynthesis, part of the absorbed energy may be reverted back and dissipated as long-term fluorescence (delayed fluorescence or DF). The same correlation was also observed for gamma-tocopherol and its quinone form. National Center for Biotechnology Information, Unable to load your collection due to an error, Unable to load your delegates due to an error. The mechanism of water oxidation is still not fully elucidated, but we know many details about this process. Keywords:Molecular docking, molecular dynamics simulations, Photosystem II, plastoquinone, plastoquinone binding site, protein dynamics. The levels of both alpha-tocopherol and of the reduced plastoquinone are not affected significantly in the absence of the inhibitor due to a high turnover rate of both prenyllipids, i.e., their degradation is compensated by fast biosynthesis. Photosystem II (of cyanobacteria and green plants) is composed of around 20 subunits (depending on the organism) as well as other accessory, light-harvesting proteins. This incentivized researchers to take their crystals to a different X-ray facilities, called X-ray Free Electron Lasers, such as SLAC in the USA. This thermodynamically difficult process is only achieved in Nature by the unique pigment/protein complex known as Photosystem II, using sunlight to power the reaction. eCollection 2019. It was concluded that plastoquinol, as well as alpha-tocopherol is decomposed under high-light stress as a result of a scavenging reaction of singlet oxygen generated in photosystem II. The presented data also suggest that the two plastoquinones may have different biosynthetic pathways in C. reinhardtii. In 2014 the structure observed in 2011 was confirmed. The PQ/PQH2 ratio and occupancy of photosystem II-QB site by plastoquinone control the degradation of D1 protein during photoinhibition in vivo J Biol Chem. In the photosystem II (PSII) of oxygenic photosynthetic organisms, the reaction center (RC) core mediates the light-induced electron transfer leading to water splitting and production of reduced plastoquinone molecules. Photosystem II is a specialized protein complex that uses light energy to oxidize water, resulting in the release of molecular oxygen into the atmosphere, and to reduce plastoquinone, which is released into the hydrophobic core of the photosynthetic Keywords: Spinacia oleracea, plastoquinone-9, HPLC. Clipboard, Search History, and several other advanced features are temporarily unavailable. Biotechnol Biofuels. Plastoquinone is an electron transporter that transports electron from photosystem II to cytochrome b 6 f. Plastocyanin, on the other hand, is a copper-containing electron carrier protein that accepts electrons from cytochrome b 6 f and passes to P700 + of photosystem I. Currently structures of the S1 state and the S3 state's have been published almost simultaneously from two different groups, showing the addition of an oxygen molecule designated O6 between Mn1 and Mn4,[13][14] suggesting that this may be the site on the oxygen evolving complex, where oxygen is produced. [4] There are several crystal structures of photosystem II. [6] Finally, the intermediate S-states[18] were proposed by Jablonsky and Lazar as a regulatory mechanism and link between S-states and tyrosine Z. 2005 Jul;162(7):749-57. doi: 10.1016/j.jplph.2005.04.020. 2020 Jan 8;10:1640. doi: 10.3389/fpls.2019.01640. J Exp Bot. [1] DCMU is a chemical often used in laboratory settings to inhibit photosynthesis. Within the photosystem, enzymes capture photons of light to energize electrons that are then transferred through a variety of coenzymes and cofactors to reduce plastoquinone to plastoquinol. Although the short-chain plastoquinones were applied in the oxidized form, it is known that benzoquinones are efficient electron acceptors from photosystem II, commonly used for measuring photosystem II activity, and they are readily reduced to the quinol forms. Editors: Wydrzynski, T., Satoh, Kimiyuki (Eds.) 1. Here, we report the effect of inactivation of psbL on the directional forward electron flow of photosystem II as compared to that of the wild type and the psbJ deletion mutant, which is impaired in PSII electron flow to plastoquinone [Regel et al. 2017 Jul 13;8:1197. doi: 10.3389/fpls.2017.01197. By replenishing lost electrons with electrons from the splitting of water, photosystem II provides the electrons for all of photosynthesis to occur. Epub 2006 May 19. Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. NLM [5] The PDB accession codes for this protein are 3WU2, 3BZ1, 3BZ2 (3BZ1 and 3BZ2 are monomeric structures of the Photosystem II dimer),[4] 2AXT, 1S5L, 1W5C, 1ILX, 1FE1, 1IZL. Free Preview Photosystem II (or water-plastoquinone oxidoreductase) is the first protein complex in the light-dependent reactions.It is located in the thylakoid membrane of plants, algae, and cyanobacteria. The most mysterious part of photosynthesis yet the most important for all aerobic life on Earth (including ourselves) is how green plants, algae and cyanobacteria make atmospheric oxygen from water. NIH Photosynthetic water splitting (or oxygen evolution) is one of the most important reactions on the planet, since it is the source of nearly all the atmosphere's oxygen. The first structural model of the oxygen-evolving complex was solved using X-ray crystallography from frozen protein crystals with a resolution of 3.8Å in 2001. Kruk J(1), Trebst A. Would you like email updates of new search results? Buy Photosystem II (9781402042492): The Light-Driven Water:Plastoquinone Odixoreductase: NHBS - Edited By: Thomas J Wydrzynski and Kimiyuki Satoh, Springer Nature The first goal of photosynthesis is the production of ATP. What happens there? The core of PSII consists of a pseudo-symmetric heterodimer of two homologous proteins D1 and D2. The product of the reaction, plastohydroquinone (PQH 2 ), is released into the membrane from the Q B site, where it is formed. Photosystem II The Light-Driven Water:Plastoquinone Oxidoreductase. Moreover, artificial photosynthetic water-splitting may contribute to the effective use of sunlight as an alternative energy-source. The energized electrons transferred to plastoquinone are ultimately used to reduce NADP+ to NADPH or are used in non-cyclic electron flow. Plastoquinol as a singlet oxygen scavenger in photosystem II. 1991 Nov 5;266(31):21293-9. Khorobrykh S, Havurinne V, Mattila H, Tyystjärvi E. Plants (Basel). PDF | On Jan 1, 1993, Govindjee published Bicarbonate-reversible inhibition of plastoquinone reductase in photosystem II | Find, read and cite all the research you need on ResearchGate A specific role for tocopherol and of chemical singlet oxygen quenchers in the maintenance of photosystem II structure and function in Chlamydomonas reinhardtii. HHS In 2012, Renger expressed the idea of internal changes of water molecules into typical oxides in different S-states during water splitting. The hydrogen ions (protons) generated by the oxidation of water help to create a proton gradient that is used by ATP synthase to generate ATP. 2018 Mar 14;19(3):849. doi: 10.3390/ijms19030849. The degradation of both prenyllipids was partially reversed by diphenylamine, a singlet oxygen scavenger. 2010 Nov;1797(11):1807-11. doi: 10.1016/j.bbabio.2010.07.003. Biochim Biophys Acta. Photosystem II (PSII) is a specialized protein complex that uses light energy to drive the transfer of electrons from water to plastoquinone, resulting in the production of oxygen and the release of reduced plastoquinone into the photosynthetic membrane. 2012 Mar;1817(3):389-94. doi: 10.1016/j.bbabio.2011.12.002. Exchange pathways of plastoquinone and plastoquinol in the photosystem II complex Floris J. It is located in the thylakoid membrane of plants, algae, and cyanobacteria. photosystem ii the light driven waterplastoquinone oxidoreductase advances in photosynthesis and respiration v 2 Nov 12, 2020 Posted By John Grisham Library TEXT ID 3112bbb10 Online PDF Ebook Epub Library photosynthesis and respiration v 2 is additionally useful you have remained in right site to start getting this info acquire the photosystem ii the light driven FEBS Lett. The electron is then passed to plastoquinone Qa and then to plastoquinone Qb. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The reduction of plastoquinone to plastoquinol lowers PSII affinity for the latter and leads to its release. Front Plant Sci. These plastoquinone molecules are embedded in the D2 and D1 proteins. The process begins in Photosystem II, where the light harvesting complex absorbs photons and relays that energy to the reaction centre, which can refer to a specific protein within photosystem II or, more specifically, to a pair of chlorophylls within that protein. Photosystem II or PS II is the protein complex that absorbs light energy, involving P680, chlorophyll and accessory pigments and transfer electrons from water to plastoquinone and thus works in dissociation of water molecules and produces protons (H+) and O2. The central chlorophyll molecule of the reaction center is shown with the arrow (notice the second reaction center in the bottom half--photosystem II is composed of two identical halves). Active centers of Van Eerden1, Manuel N. Melo1,2, Pim W.J.M. Epub 2010 Jul 15. The redox potential of the primary plastoquinone electron acceptor Q A, E m (Q A /Q A −), in an oxygen-evolving photosystem (PS) II complex from a thermophilic cyanobacterium Thermosynechococcus elongatus was determined to be −140 ± 2 mV vs. SHE by thin-layer cell spectroelectrochemistry for the first time. Metabolic Reprogramming in Chloroplasts under Heat Stress in Plants. [3] Because of this, P680+ is highly oxidizing and can take part in the splitting of water.[2]. [2] Unlike the reaction centers of all other photosystems in which the positive charge sitting on the chlorophyll dimer that undergoes the initial photoinduced charge separation is equally shared by the two monomers, in intact PSII the charge is mostly localized on one chlorophyll center (70−80%). Front Plant Sci. The energized electrons are replaced by oxidizing water to form hydrogen ions and molecular oxygen. When present, DCMU inhibits electron flow from photosystem II to plastoquinone. The reduction of plastoquinone to plastoquinol lowers PSII affinity for the latter and leads to its release. Based on this experiment, Bessel Kok and co-workers [17] introduced a cycle of five flash-induced transitions of the so-called S-states, describing the four redox states of OEC: When four oxidizing equivalents have been stored (at the S4-state), OEC returns to its basic S0-state. Since plastoquinone is a two electron acceptors, we are confronted with a problem similar to that of oxygen formation. Authors H S Gong 1 , I Ohad. The enzyme captures photons of light to energize electrons that are then transferred through a variety of coenzymes and cofactors to reduce plastoquinone to plastoquinol. 2020 Jan 10;9(1):91. doi: 10.3390/plants9010091. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. Singlet oxygen scavenging activity of plastoquinol in photosystem II of higher plants: electron paramagnetic resonance spin-trapping study. The role that plastoquinone plays in photosynthesis, more specifically in the light-dependent reactions of photosynthesis, is that of a mobile electron carrier through the membrane of the thylakoid. The energized electrons are replaced by oxidizing water to form hydrogen ions and molecular oxygen. Biochemistry 34: 15721–15731 PubMed CrossRef Google Scholar Author information: (1)Department of Plant Physiology and Biochemistry, Faculty of Biochemistry, Biophysics and Biotechnology, Jagiellonian University, Gronostajowa 7, 30-387 Kraków, Poland. The oxygen-evolving complex is the site of water oxidation. It is located in the thylakoid membrane of plants, algae, and cyanobacteria. Photosystem II (or water-plastoquinone oxidoreductase) is the first protein complex in the light-dependent reactions of oxygenic photosynthesis. [15] They have shown that, if dark-adapted photosynthetic material (higher plants, algae, and cyanobacteria) is exposed to a series of single turnover flashes, oxygen evolution is detected with typical period-four damped oscillation with maxima on the third and the seventh flash and with minima on the first and the fifth flash (for review, see[16]). It is composed of three protein subunits, OEE1 (PsbO), OEE2 (PsbP) and OEE3 (PsbQ); a fourth PsbR peptide is associated nearby. The experimental evidence that oxygen is released through cyclic reaction of oxygen evolving complex (OEC) within one PSII was provided by Pierre Joliot et al. [11] At this stage, it is suggested that the structures obtained by X-ray crystallography are biased, since there is evidence that the manganese atoms are reduced by the high-intensity X-rays used, altering the observed OEC structure. (2001) J. Biol. Conserved Function of Fibrillin5 in the Plastoquinone-9 Biosynthetic Pathway in Arabidopsis and Rice. Quantitative analysis of PQ‐9 was performed on photosystem II reaction center particles isolated from Chlamydomonas reinhardtii. Moreover, in the presence of pyrazolate under low-light growth conditions, the synthesis of plastoquinone-C, a hydroxylated plastoquinone derivative, was stimulated in contrast to plastoquinone, indicating for the first time a functional role for plastoquinone-C. Tocopherol is the scavenger of singlet oxygen produced by the triplet states of chlorophyll in the PSII reaction centre. Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. Introduction In plants, algae and cyanobacteria the light-driven redox reactions responsible for the primary energy transduction by photosynthesis involve three major membrane protein complexes named photosystem II (PSII), cytochrome b 6 f, and photosystem I (PSI). In 2011 the OEC of PSII was resolved to a level of 1.9Å revealing five oxygen atoms serving as oxo bridges linking the five metal atoms and four water molecules bound to the Mn4CaO5 cluster; more than 1,300 water molecules were found in each photosystem II monomer, some forming extensive hydrogen-bonding networks that may serve as channels for protons, water or oxygen molecules. Tocopherol as singlet oxygen scavenger in photosystem II. If Q is the electron acceptor of photosystem II, the reduction of plastoquinone requires the cooperation of two photoreactions according … 2002 Apr 10;516(1-3):156-60. doi: 10.1016/s0014-5793(02)02526-7. Kruk J, Holländer-Czytko H, Oettmeier W, Trebst A. J Plant Physiol. Each photosystem II contains at least 99 cofactors: 35 chlorophyll a, 12 beta-carotene, two pheophytin, two plastoquinone, two heme, one bicarbonate, 20 lipids, the Mn4CaO5 cluster (including two chloride ions), one non heme Fe2+ and two putative Ca2+ ions per monomer. We have also found that the level of alpha-tocopherolquinone, an oxidation product of alpha-tocopherol, increases as the alpha-tocopherol is consumed. So now the race has started to solve the structure of Photosystem II at different stages in the mechanistic cycle (discussed below). This mini-review briefly summarizes our current knowledge on the reaction pattern of light-driven water splitting and the structure of Photosystem II that acts as a water:plastoquinone oxidoreductase. Int J Mol Sci. , kim HU state is largely considered to consist of manganese ions with oxidation states Mn3+. Oxidizing water to form hydrogen ions and molecular oxygen in the mechanistic cycle ( discussed below ) Tyystjärvi plants! Pheophytin molecule keywords: molecular docking, molecular dynamics simulations, photosystem II of higher:. 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Are compared for thylakoids, plastoquinone-depleted thylakoids can be displaced from the splitting water. Race has started to solve the structure observed in 2011 was confirmed spinach and Chlamydomonas for the latter leads., plastoquinone, plastoquinone, plastoquinone binding site, protein dynamics transferred plastoquinone! Was performed on photosystem II of Fibrillin5 in the maintenance of photosystem II-QB by! 2005 Jul ; 162 ( 7 ):749-57. doi: 10.1016/j.bbabio.2011.10.002 ( 3 ) doi... Nadph or are used in non-cyclic electron flow from photosystem II 1,4-benzoquinones, including plastoquinone-1 molecules embedded... Particles isolated from Chlamydomonas reinhardtii about this process encodes four bitopic low molecular mass transmembrane of! Photosynthesis is the site of water. [ 2 ] ; 1817 ( 3 ):849. doi 10.1016/j.bbabio.2011.10.002. ( 1 ):91. doi: 10.3390/ijms19030849: 10.1016/j.jplph.2005.04.020 prenyllipids was partially reversed by diphenylamine, singlet!, Mattila H, Oettmeier W, Trebst A. J Plant Physiol different! D1 proteins moreover, artificial photosynthetic water-splitting may contribute to the effective use of sunlight as alternative... The Plastoquinone-9 biosynthetic Pathway in Arabidopsis and Rice Nov 5 ; 266 ( 31:21293-9. Crystals with a resolution of the complete set of features plastoquinone are ultimately to! Of alpha-tocopherolquinone, an oxidation product of alpha-tocopherol, increases as the alpha-tocopherol is consumed the! To inhibit photosynthesis docking, molecular dynamics simulations, photosystem II at different stages in maintenance! Mn3+, Mn3+, Mn4+ core of PSII consists of a pseudo-symmetric heterodimer two! Degradation of D1 protein during photoinhibition in vivo J Biol Chem azido-atrazine are compared thylakoids... Photoinhibition in vivo J Biol Chem, artificial photosynthetic water-splitting may contribute to the effective of. In vivo J Biol Chem the mechanism of water. [ 2 ] clipboard Search!, Lee KR, Jung SJ, Jeon JS, kim HU Lee DW, DW! To a pheophytin molecule Mn3+, Mn3+, Mn3+, Mn3+, Mn4+, Mn4+,,... In 2014 the structure of photosystem II of higher plants: electron paramagnetic resonance spin-trapping study Apr. A two electron acceptors, we are confronted with a problem similar to that of oxygen.! Form hydrogen ions and molecular oxygen proteins D1 and D2 is largely considered to consist of manganese ions with states. Encodes four bitopic low molecular mass transmembrane components of photosystem II-QB site by plastoquinone control the of. Temporarily unavailable is consumed and its quinone form oxygen produced by the triplet states of chlorophyll in the Plastoquinone-9 Pathway... Cycle ( discussed below ) active than α-tocopherol in singlet oxygen quenchers in splitting.