Two sites for adenosine triphosphate formation in photosynthetic electron transport mediated by photosystem I. Evidence from digitonin subchloroplast particles

Biochemistry ◽  
1971 ◽  
Vol 10 (5) ◽  
pp. 866-873 ◽  
Author(s):  
Joseph Neumann ◽  
Charles J. Arntzen ◽  
Richard A. Dilley
Keyword(s):  
Electron Transport ◽  
Adenosine Triphosphate ◽  
Photosystem I ◽  
Photosynthetic Electron Transport

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.

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.

The site of electron transport inhibition by bentazon (3-isopropyl-1H-2,1,3-benzothiadiazin-(4)3H-one 2,2-dioxide) in isolated chloroplasts

1982 ◽  
Vol 60 (4) ◽  
pp. 409-412 ◽  
Author(s):  
Rungsit Suwanketnikom ◽  
Kriton K. Hatzios ◽  
Donald Penner ◽  
Duncan Bell
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Photosystem I ◽  
Electron Acceptor ◽  
Photosynthetic Electron Transport ◽  
Primary Electron ◽  
Photochemical Reactions ◽  
Spinacea Oleracea ◽  
Primary Electron Acceptor ◽  
Isolated Chloroplasts

The effect of bentazon (3-isopropyl-1H-2,1,3-benzathiadiazin-(4)3H-one 2,2-dioxide) on various photochemical reactions of isolated spinach (Spinacea oleracea L.) chloroplasts was studied at concentrations 0, 5, 15, 45, and 135 μM. Bentazon at a concentration of 135 μM strongly inhibited uncoupled electron transport from water to ferricyanide or to methylviologen with inhibition percentages greater than 90%. Photosystem II mediated electron transport from water to oxidized diaminodurene, with 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone (DBMIB) blocking photosystem I, was also strongly inhibited by bentazon at 135 μM but less with lower concentrations of bentazon. Photosystem I mediated transfer of electrons from diaminodurene to methylviologen, with 3,4-dichlorophenyl-1,1-dimethylurea (DCMU) blocking photosystem II, was not inhibited by bentazon at any concentration examined. Transfer of electrons from catechol to methylviologen in hydroxylamine-treated chloroplasts was inhibited by bentazon, and the inhibition percentages were again concentration dependent. The data indicate that the site of bentazon inhibition of the photosynthetic electron transport is at the reducing side of photosystem II, between the primary electron acceptor Q and plastoquinone.

scholarly journals The effects of high concentrations of salts on photosynthetic electron transport in spinach (Spinacia oleracea) chloroplasts

1982 ◽  
Vol 204 (3) ◽  
pp. 705-712 ◽  
Author(s):  
A C Stewart
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Photosystem I ◽  
Spinacia Oleracea ◽  
Photosynthetic Electron Transport ◽  
Potassium Citrate ◽  
O2 Evolution ◽  
Hofmeister Series ◽  
Reaction Centre ◽  
High Concentrations

1. Photosynthetic electron transport from water to lipophilic Photosystem II acceptors was stimulated 3-5-fold by high concentrations (greater than or equal to 1 M) of salts containing anions such as citrate, succinate and phosphate that are high in the Hofmeister series. 2. In trypsin-treated chloroplasts, K3Fe(CN)6 reduction insensitive to 3-(3,4-dichlorophenyl)-1,1-dimethylurea was strongly stimulated by high concentrations of potassium citrate, but there was much less stimulation of 2,6-dichloroindophenol reduction in Tris-treated chloroplasts supplied with 1,5-diphenylcarbazide as artificial donor. The results suggest that the main site of action of citrate was the O2-evolving complex of Photosystem II. 3. Photosystem I partial reactions were also stimulated by intermediate concentrations of citrate (up to 2-fold stimulation by 0.6-0.8 M-citrate), but were inhibited at the highest concentrations. The observed stimulation may have been caused by stabilizaton of plastocyanin that was complexed with the Photosystem I reaction centre, 4. At 1 M, potassium citrate protected O2 evolution against denaturation by heat or by the chaotropic agent NaNO3. 5. It is suggested that anions high in the Hofmeister series stimulated and stabilized electron transport by enhancing water structure around the protein complexes in the thylakoid membrane.

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.

Diethyldithiocarbamate, a New Photosystem I Electron Donor of Mehler-Type Hill Reactions

1986 ◽  
Vol 41 (9-10) ◽  
pp. 861-866 ◽  
Author(s):  
Brad L. Upham ◽  
Kriton K. Hatzios
Keyword(s):  
Superoxide Dismutase ◽  
Electron Transport ◽  
Electron Donor ◽  
Photosystem I ◽  
Photosynthetic Electron Transport ◽  
Mehler Reaction ◽  
Plastoquinone Pool ◽  
Electron Donation

Abstract Diethyldithiocarbamate (DEDTC) does not accept electrons from the photosynthetic electron transport (PET) but can donate electrons to a photosystem I (PSI) Mehler reaction in the pres­ence of the following PET inhibitors: DCMU. DBMIB, and bathophenanthroline. It cannot photoreduce PSI in the presence of cyanide, a PET inhibitor. These data indicate that the site of electron donation is after the plastoquinone pool. Ascorbate is not required for the ability of DEDTC to donate electrons to PSI. There is no photoreductant activity by DEDTC inferredoxin/NADP Hill reactions. Superoxide dismutase inhibits DEDTC/DCMU or bathophenanthroline→methylviologen/O2 Mehler reaction. Catalase does not recover the consumed O2 from a DEDTC/DCMU→methylviologen/O2 Mehler reaction, indicating O2- has not been dismutating into H2O2. These results indicate that superoxide is required for DEDTC ability to donate electrons, therefore DEDTC is limited only to Mehler-type reactions.

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