Reduction of the Mn Cluster of the Water-Oxidizing Enzyme by Nitric Oxide:  Formation of an S<sub>-</sub><sub>2</sub> State

Schansker, Gert; Goussias, Charilaos; Petrouleas, Vasili; Rutherford, A. William

doi:10.1021/bi015903z

Cited by 45 publications

(36 citation statements)

References 50 publications

(50 reference statements)

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“…This effect is largely prevented in the presence of PTIO (Table II). The increase in the nondecaying part of fluorescence correlates with previous results of Schansker et al (2002) showing that NO reduces the Mn cluster of the water-oxidizing complex into the S -2 state. Our measurements with GSNO indicate that Q A 2 is unable to recombine with the S 2 state, possibly because NO inactivates or reduces the Mn cluster.…”

Section: No Causes Donor and Acceptor Side Inhibition Of Psii Electrosupporting

confidence: 88%

“…The rate of electron transport may decrease on the donor side as well, since in vitro experiments have proven that NO interacts with the Y D Á Tyr residue and the water-oxidizing complex. The latter is reduced to the S 22 state by NO, as shown by oxygen electrode, fluorescence, and electron paramagnetic resonance measurements (Schansker et al, 2002). Our Q A 2 reoxidation measurements show a reduced rate of electron transport between Q A and Q B upon NO donor treatment.…”

Section: No Hinders Electron Transfer In Psii In Vivosupporting

confidence: 58%

“…Electron paramagnetic resonance and chlorophyll fluorescence measurements using NO gas treatment of isolated thylakoid membrane complexes have clearly demonstrated that NO can reversibly bind to several sites in PSII and inhibit electron transfer. Important binding sites of NO within the PSII complex are the nonheme iron between Q A and Q B binding sites , the Y D Á Tyr residue of the D2 protein (Sanakis et al, 1997), and the manganese (Mn) cluster of the water-oxidizing complex (Schansker et al, 2002). Takahashi and Yamasaki (2002) showed that the NO donor S-nitroso-N-acetylpenicillinamine (SNAP) does not modify the maximal quantum efficiency (F v /F m ), but inhibits the linear electron transport rate, DpH formation across the thylakoid membrane, and decreases the rate of ATP synthesis.…”

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confidence: 99%

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In Vivo Target Sites of Nitric Oxide in Photosynthetic Electron Transport as Studied by Chlorophyll Fluorescence in Pea Leaves

et al. 2008

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The role of nitric oxide (NO) in photosynthesis is poorly understood as indicated by a number of studies in this field with often conflicting results. As various NO donors may be the primary source of discrepancies, the aim of this study was to apply a set of NO donors and its scavengers, and examine the effect of exogenous NO on photosynthetic electron transport in vivo as determined by chlorophyll fluorescence of pea (Pisum sativum) leaves. Sodium nitroprusside-induced changes were shown to be mediated partly by cyanide, and S-nitroso-N-acetylpenicillinamine provided low yields of NO. However, the effects of S-nitrosoglutathione are inferred exclusively by NO, which made it an ideal choice for this study. Q A 2 reoxidation kinetics show that NO slows down electron transfer between Q A and Q B , and inhibits charge recombination reactions of Q A 2 with the S 2 state of the water-oxidizing complex in photosystem II. Consistent with these results, chlorophyll fluorescence induction suggests that NO also inhibits steady-state photochemical and nonphotochemical quenching processes. NO also appears to modulate reaction-center-associated nonphotochemical quenching.Plants, as well as animals, respond to ambient levels of nitric oxide (NO), and also generate NO themselves via various enzymatic and nonenzymatic pathways (Yamasaki, 2000;Neill et al., 2003;Río et al., 2004). Indeed, in the past years, a growing amount of research has provided evidence for the multiple physiological roles of this gaseous free radical in plants (for review, see Wendehenne et al., 2004;Delledonne, 2005). The turnover of NO depends on its concentration, the ambient redox status, and the concentration of target molecules. In biological systems, NO is capable of targeting thiol-and metal-containing proteins (Lamattina et al., 2003). Photosynthetic and mitochondrial electron transport chains are abundant in transition metalcontaining complexes, and NO and its derivative peroxynitrite are known to inhibit the mitochondrial electron transport chain (Millar and Day, 1996;Yamasaki et al., 2001). Yet, the effect of exogenous NO on photosynthetic activity in intact leaves has so far been poorly addressed, with often conflicting results.Previous research suggests that NO gas decreases net photosynthesis rates in oat (Avena sativa) and alfalfa (Medicago sativa) leaves (Hill and Bennett, 1970). Lum et al. (2005) have identified a number of intracellular targets of NO signalization including mitochondria, peroxisomes, and chloroplasts. They found that the NO donor sodium nitroprusside (SNP) decreases the amount of Rubisco activase and the b-subunit of the Rubisco subunit-binding protein in mung bean (Phaseolus aureus).NO is also able to influence the photosynthetic electron transport chain directly. An important action site of NO is PSII. Electron paramagnetic resonance and chlorophyll fluorescence measurements using NO gas treatment of isolated thylakoid membrane complexes have clearly demonstrated that NO can reversibly bind to several sites in PSII and...

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Section: No Causes Donor and Acceptor Side Inhibition Of Psii Electrosupporting

confidence: 88%

Section: No Hinders Electron Transfer In Psii In Vivosupporting

confidence: 58%

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confidence: 99%

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In Vivo Target Sites of Nitric Oxide in Photosynthetic Electron Transport as Studied by Chlorophyll Fluorescence in Pea Leaves

et al. 2008

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“…Although the concentrations of methanol used in this study did not interfere with PSII activity, they modify the spectroscopic properties of oxidation states of the Mn-cluster (e.g. see Messinger et al, 1997;Schansker et al, 2002).…”

Section: Measurements Of Photosynthetic Activitymentioning

confidence: 89%

Polyphenolic Allelochemicals from the Aquatic Angiosperm Myriophyllum spicatumInhibit Photosystem II

et al. 2002

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Myriophyllum spicatum (Haloragaceae) is a highly competitive freshwater macrophyte that produces and releases algicidal and cyanobactericidal polyphenols. Among them, ␤-1,2,3-tri-O-galloyl-4,6-(S)-hexahydroxydiphenoyl-d-glucose (tellimagrandin II) is the major active substance and is an effective inhibitor of microalgal exoenzymes. However, this mode of action does not fully explain the strong allelopathic activity observed in bioassays. Lipophilic extracts of M. spicatum inhibit photosynthetic oxygen evolution of intact cyanobacteria and other photoautotrophs. Fractionation of the extract provided evidence for tellimagrandin II as the active compound. Separate measurements of photosystem I and II activity with spinach (Spinacia oleracea) thylakoid membranes indicated that the site of inhibition is located at photosystem II (PSII). In thermoluminescence measurements with thylakoid membranes and PSII-enriched membrane fragments M. spicatum extracts shifted the maximum temperature of the B-band (S 2 Q B Ϫ recombination) to higher temperatures. Purified tellimagrandin II in concentrations as low as 3 m caused a comparable shift of the B-band. This demonstrates that the target site of this inhibitor is different from the Q B -binding site, a common target of commercial herbicides like 3-(3,4-dichlorophenyl)-1,1-dimethylurea. Measurements with electron paramagnetic resonance spectroscopy suggest a higher redox midpoint potential for the non-heme iron, located between the primary and the secondary quinone electron acceptors, Q A and Q B . Thus, tellimagrandin II has at least two modes of action, inhibition of exoenzymes and inhibition of PSII. Multiple target sites are a common characteristic of many potent allelochemicals. Allelopathy (sensu;Molisch, 1937) is considered an effective trait of submerged aquatic angiosperms (Wium-Andersen, 1987; Gross, 1999, and refs. therein) to counteract the usually strong competition for light and carbon with other primary producers, especially phytoplankton and epiphytes (SandJensen and Søndergaard, 1981). Allelopathically active compounds known from terrestrial plants generally act as natural herbicides and often have multiple effects on the metabolism of target organisms (Einhellig, 2001). Some have even been explored as natural substitutes for commercial herbicides (Duke et al., 2000). Few studies have, however, targeted the mode of action of allelochemicals from aquatic angiosperms.Several allelochemicals isolated from cyanobacteria or higher plants specifically inhibit photosynthesis of target organisms (Einhellig et al., 1993;Gonzalez et al., 1997;Smith and Doan, 1999). This results in a lower primary production and might consequently cause slower growth of competing photoautotrophs. To prove effects on primary production, the radiocarbon assay (fixation of radioactive labeled 14 C) has been frequently used, e.g. with extracts from Zostera marina (Harrison and Durance, 1985) and Chara globularis (Wium-Andersen et al., 1983). More detailed studies involved separate measureme...

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“…Nitric oxide is able to influence the photosynthetic electron transport chain directly. PS II is an important site for NO action [101]; within PS II complex, important binding sitesofNOarethenonheme ironbetweenQ A andQ B bindingsites [102],Y D , Tyrresidue of D2 protein [103], and manganese (Mn) cluster of water-oxidizing complex [104].…”

Section: Effect Of Nitric Oxide On Photosynthesismentioning

confidence: 99%

Nitric Oxide: Chemistry, Biosynthesis, and Physiological Role

Hayat

Hasan

Mori

et al. 2009

Nitric Oxide in Plant Physiology

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SummaryNO is recognized as a biological messenger in plants. It is a highly reactive gaseous free radical, soluble in water and lipid. It can be synthesized in plants via different enzymatic and nonenzymatic sources such as NOS, NR, XOR, and Ni-NOR. Due to its high lipophilic nature, it can easily diffuse through membrane and can act as a inter-and intracellular messenger and regulate diverse physiological and biochemical processes in plants in a concentration-dependent manner, such as seed dormancy, growth and development, senescence, respiration, photosynthesis, programmed cell death, antioxidant defense system, and so on. Moreover, NO also has an ability to act simultaneously with other molecules and signals in plants. This chapter covers the advances in chemical properties and mechanism of its biosynthesis with special emphasis on the role of NO in the physiological and biochemical changes that occur in plants under normal conditions due to the exogenously applied or endogenously produced NO, along with the cross talk between NO and other phytohormones. 1.1

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Reduction of the Mn Cluster of the Water-Oxidizing Enzyme by Nitric Oxide: Formation of an S_-₂ State

Cited by 45 publications

References 50 publications

In Vivo Target Sites of Nitric Oxide in Photosynthetic Electron Transport as Studied by Chlorophyll Fluorescence in Pea Leaves

In Vivo Target Sites of Nitric Oxide in Photosynthetic Electron Transport as Studied by Chlorophyll Fluorescence in Pea Leaves

Polyphenolic Allelochemicals from the Aquatic Angiosperm Myriophyllum spicatumInhibit Photosystem II

Nitric Oxide: Chemistry, Biosynthesis, and Physiological Role

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Reduction of the Mn Cluster of the Water-Oxidizing Enzyme by Nitric Oxide: Formation of an S-2 State

Cited by 45 publications

References 50 publications

In Vivo Target Sites of Nitric Oxide in Photosynthetic Electron Transport as Studied by Chlorophyll Fluorescence in Pea Leaves

In Vivo Target Sites of Nitric Oxide in Photosynthetic Electron Transport as Studied by Chlorophyll Fluorescence in Pea Leaves

Polyphenolic Allelochemicals from the Aquatic Angiosperm Myriophyllum spicatumInhibit Photosystem II

Nitric Oxide: Chemistry, Biosynthesis, and Physiological Role

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Reduction of the Mn Cluster of the Water-Oxidizing Enzyme by Nitric Oxide: Formation of an S_-₂ State