scholarly journals Regulation of electron transport is essential for photosystem I stability and plant growth

2019 ◽  
Author(s):  
Mattia Storti ◽  
Anna Segalla ◽  
Marco Mellon ◽  
Alessandro Alboresi ◽  
Tomas Morosinotto
Keyword(s):  
Electron Transport ◽  
Photosystem I ◽  
Nadh Dehydrogenase ◽  
Physcomitrella Patens ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Type I ◽  
Growth Reduction ◽  
Light Regimes ◽  
Photosynthetic Organisms

AbstractLife depends on the ability of photosynthetic organisms to exploit sunlight to fix carbon dioxide into biomass. Photosynthesis is modulated by pathways such as cyclic and pseudocyclic electron flow (CEF and PCEF). CEF transfers electrons from photosystem I to the plastoquinone pool according to two mechanisms, one dependent on proton gradient regulators (PGR5/PGRL1) and the other on the type I NADH dehydrogenase (NDH) complex. PCEF uses electrons from photosystem I to reduce oxygen; in several groups of photosynthetic organisms but not in angiosperms, it is sustained by flavodiiron proteins (FLVs). PGR5/PGRL1, NDH and FLVs are all active in the moss Physcomitrella patens, and mutants depleted in these proteins show phenotypes under specific light regimes. Here, we demonstrated that CEF and PCEF exhibit strong functional overlap and that when one protein component is depleted, the others can compensate for most of the missing activity. When multiple mechanisms are simultaneously inactivated, however, plants show damage to photosystem I and strong growth reduction, demonstrating that mechanisms for the modulation of photosynthetic electron transport are indispensable.

scholarly journals Flavodiiron proteins act as safety valve for electrons in Physcomitrella patens

2016 ◽  
Vol 113 (43) ◽  
pp. 12322-12327 ◽  
Author(s):  
Caterina Gerotto ◽  
Alessandro Alboresi ◽  
Andrea Meneghesso ◽  
Martina Jokel ◽  
Marjaana Suorsa ◽  
...  
Keyword(s):  
Electron Transport ◽  
Photosystem I ◽  
Physcomitrella Patens ◽  
Safety Valve ◽  
Cell Metabolism ◽  
Photosynthetic Apparatus ◽  
Photosynthetic Electron Transport ◽  
Flowering Plants ◽  
Knock Out ◽  
Electron Sink

Photosynthetic organisms support cell metabolism by harvesting sunlight to fuel the photosynthetic electron transport. The flow of excitation energy and electrons in the photosynthetic apparatus needs to be continuously modulated to respond to dynamics of environmental conditions, and Flavodiiron (FLV) proteins are seminal components of this regulatory machinery in cyanobacteria. FLVs were lost during evolution by flowering plants, but are still present in nonvascular plants such as Physcomitrella patens. We generated P. patens mutants depleted in FLV proteins, showing their function as an electron sink downstream of photosystem I for the first seconds after a change in light intensity. flv knock-out plants showed impaired growth and photosystem I photoinhibition when exposed to fluctuating light, demonstrating FLV’s biological role as a safety valve from excess electrons on illumination changes. The lack of FLVs was partially compensated for by an increased cyclic electron transport, suggesting that in flowering plants, the FLV’s role was taken by other alternative electron routes.

Rewiring photosynthesis: a photosystem I-hydrogenase chimera that makes H2in vivo

2020 ◽  
Vol 13 (9) ◽  
pp. 2903-2914 ◽  
Author(s):  
Andrey Kanygin ◽  
Yuval Milrad ◽  
Chandrasekhar Thummala ◽  
Kiera Reifschneider ◽  
Patricia Baker ◽  
...  
Keyword(s):  
Electron Transport ◽  
Hydrogen Production ◽  
Photosystem I ◽  
Electron Transport Chain ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Photosynthetic Electron Transport Chain ◽  
Transport Chain

Photosystem I-hydrogenase chimera intercepts electron flow directly from the photosynthetic electron transport chain and directs it to hydrogen production.

scholarly journals Molecular Mechanism of Oxidation of P700 and Suppression of ROS Production in Photosystem I in Response to Electron-Sink Limitations in C3 Plants

Antioxidants ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 230 ◽  
Author(s):  
Chikahiro Miyake
Keyword(s):  
Electron Transport ◽  
Molecular Mechanism ◽  
Transport System ◽  
Photosystem I ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Electron Transport System ◽  
C3 Plants ◽  
Ros Production ◽  
Acceptor Side

Photosynthesis fixes CO2 and converts it to sugar, using chemical-energy compounds of both NADPH and ATP, which are produced in the photosynthetic electron transport system. The photosynthetic electron transport system absorbs photon energy to drive electron flow from Photosystem II (PSII) to Photosystem I (PSI). That is, both PSII and PSI are full of electrons. O2 is easily reduced to a superoxide radical (O2−) at the reducing side, i.e., the acceptor side, of PSI, which is the main production site of reactive oxygen species (ROS) in photosynthetic organisms. ROS-dependent inactivation of PSI in vivo has been reported, where the electrons are accumulated at the acceptor side of PSI by artificial treatments: exposure to low temperature and repetitive short-pulse (rSP) illumination treatment, and the accumulated electrons flow to O2, producing ROS. Recently, my group found that the redox state of the reaction center of chlorophyll P700 in PSI regulates the production of ROS: P700 oxidation suppresses the production of O2− and prevents PSI inactivation. This is why P700 in PSI is oxidized upon the exposure of photosynthesis organisms to higher light intensity and/or low CO2 conditions, where photosynthesis efficiency decreases. In this study, I introduce a new molecular mechanism for the oxidation of P700 in PSI and suppression of ROS production from the robust relationship between the light and dark reactions of photosynthesis. The accumulated protons in the lumenal space of the thylakoid membrane and the accumulated electrons in the plastoquinone (PQ) pool drive the rate-determining step of the P700 photo-oxidation reduction cycle in PSI from the photo-excited P700 oxidation to the reduction of the oxidized P700, thereby enhancing P700 oxidation.

Inhibition of Photosynthetic Electron Transport by Halogenated 4-Hydroxy-pyridines

1985 ◽  
Vol 40 (5-6) ◽  
pp. 391-399 ◽  
Author(s):  
A. Trebst ◽  
B. Depka ◽  
S. M. Ridley ◽  
A. F. Hawkins
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Photosystem I ◽  
Electron Flow ◽  
Essential Element ◽  
Photosynthetic Electron Transport ◽  
Cyclic Electron Flow ◽  
Acceptor Side

Abstract Herbicidal halogen substituted 4-hydroxypyridines are inhibitors of photosynthetic electron flow in isolated thylakoid membranes by interfering with the acceptor side of photosystem II. Tetrabromo-4-hydroxypyridine, the most active compound found, has a pI50-value of 7.6 in the inhibition of oxygen evolution in both the reduction of an acceptor of photosystem I and an acceptor of photosystem II. The new inhibitors displace both metribuzin and ioxynil from the membrane. The 4-hydroxypyridines, like ioxynil, have unimpaired inhibitor potency in Tristreated chloroplasts, whereas the DCMU-type family of herbicides does not. It is suggested that 4-hydroxypyridines are complementary to phenol-type inhibitors, and a common essential element is proposed. The 4-hydroxypyridines do not inhibit photosystem I or non-cyclic electron flow through the cytochrome b/f complex. But they do have a second inhibition site in photosynthetic electron transport since they inhibit ferredoxin-catalyzed cyclic electron flow, indicating an antimycin-like property. A comparison of the in vitro potency of the compounds with the in vivo potency shows no correlation. A major herbicidal mode of action of the group is related to the inhibition of carotenoid synthesis, and access to the chloroplast lamellae in vivo for inhibition of electron transport may be restricted.

scholarly journals Photosystem I cyclic electron flow via chloroplast NADH dehydrogenase-like complex performs a physiological role for photosynthesis at low light

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Wataru Yamori ◽  
Toshiharu Shikanai ◽  
Amane Makino
Keyword(s):  
Electron Transport ◽  
Light Intensity ◽  
Photosystem I ◽  
Nadh Dehydrogenase ◽  
Physiological Function ◽  
Electron Flow ◽  
Cyclic Electron Flow ◽  
Cyclic Electron Transport ◽  
Low Light ◽  
Ps I

Abstract Cyclic electron transport around photosystem I (PS I) was discovered more than a half-century ago and two pathways have been identified in angiosperms. Although substantial progress has been made in understanding the structure of the chloroplast NADH dehydrogenase-like (NDH) complex, which mediates one route of the cyclic electron transport pathways, its physiological function is not well understood. Most studies focused on the role of the NDH-dependent PS I cyclic electron transport in alleviation of oxidative damage in strong light. In contrast, here it is shown that impairment of NDH-dependent cyclic electron flow in rice specifically causes a reduction in the electron transport rate through PS I (ETR I) at low light intensity with a concomitant reduction in CO2 assimilation rate, plant biomass and importantly, grain production. There was no effect on PS II function at low or high light intensity. We propose a significant physiological function for the chloroplast NDH at low light intensities commonly experienced during the reproductive and ripening stages of rice cultivation that have adverse effects crop yield.

Superoxide-and Ethane-Formation in Subchloroplast Particles: Catalysis by Pyridinium Derivatives

1980 ◽  
Vol 35 (9-10) ◽  
pp. 770-775 ◽  
Author(s):  
E. F. Elstner ◽  
H. P. Fischer ◽  
W. Osswald ◽  
G. Kwiatkowski
Keyword(s):  
Electron Transport ◽  
Photosystem I ◽  
Photosynthetic Electron Transport ◽  
Redox Potentials ◽  
Light Reaction ◽  
Pyridinium Bromide ◽  
Superoxide Formation ◽  
Fatty Acid Peroxidation ◽  
Chlorophyll Bleaching ◽  
Ethane Formation

Abstract Oxygen reduction by chloroplast lamellae is catalyzed by low potential redox dyes with E′0 values between -0 .3 8 V and -0 .6 V. Compounds of E′0 values of -0 .6 7 V and lower are inactive. In subchloroplast particles with an active photosystem I but devoid of photosynthetic electron transport between the two photosystems, the active redox compounds enhance chlorophyll bleaching, superoxide formation and ethane production independent on exogenous substrates or electron donors. The activities of these compounds decrease with decreasing redox potential, with one exception: 1-methyl-4,4′-bipyridini urn bromide with an E′0 value of lower -1 V (and thus no electron acceptor of photosystem I in chloroplast lamellae with intact electron transport) stimulates light dependent superoxide formation and unsaturated fatty acid peroxidation in sub­ chloroplast particles, maximal rates appearing after almost complete chlorophyll bleaching. Since this activity is not visible with compounds with redox potentials below -0 .6 V lacking the nitrogen atom at the 1-position of the pyridinium substituent, we assume that 1 -methyl-4,4′-bi-pyridinium bromide is “activated” by a yet unknown light reaction.

Interaction of Photosystem II Herbicides with Bicarbonate and Formate in Their Effects on Photosynthetic Electron Flow

1984 ◽  
Vol 39 (5) ◽  
pp. 374-377 ◽  
Author(s):  
J. J. S. van Rensen
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Electron Flow ◽  
Photosynthetic Electron Transport ◽  
Hill Reaction ◽  
Amaranthus Hybridus ◽  
Apparent Affinity ◽  
Photosynthetic Electron Flow ◽  
Different Characteristics ◽  
The Hill

The reactivation of the Hill reaction in CO2-depleted broken chloroplasts by various concentrations of bicarbonate was measured in the absence and in the presence of photosystem II herbicides. It appears that these herbicides decrease the apparent affinity of the thylakoid membrane for bicarbonate. Different characteristics of bicarbonate binding were observed in chloroplasts of triazine-resistant Amaranthus hybridus compared to the triazine-sensitive biotype. It is concluded that photosystem II herbicides, bicarbonate and formate interact with each other in their binding to the Qв-protein and their interference with photosynthetic electron transport.

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