Plastoquinol and Other Natural Membrane Prenyllipids May Form Pseudocyclic Electron Transport by Scavenging Superoxide Generated in Photosystem I

2003 ◽  
pp. 365-368
Author(s):  
J. Kruk ◽  
M. Jemioła-Rzemińska
Keyword(s):  
Electron Transport ◽  
Photosystem I

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.

Photoinhibition of Electron Transport Activity of Photosystem II in Isolated Thylakoids Studied by Thermoluminescence and Delayed Luminescence

1988 ◽  
Vol 43 (11-12) ◽  
pp. 871-876 ◽  
Author(s):  
Imre Vass ◽  
Narendranath Mohanty ◽  
Sándor Demeter
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Photosystem I ◽  
Half Life ◽  
Delayed Luminescence ◽  
Transport Activity ◽  
Primary Target ◽  
Electron Transport Activity ◽  
The Stability ◽  
Spinach Thylakoids

Abstract The effect of photoinhibition on the primary (QA) and secondary (QB) quinone acceptors of photosystem I I was investigated in isolated spinach thylakoids by the methods of thermoluminescence and delayed luminescence. The amplitudes of the Q (at about 2 °C) and B (at about 30 °C) thermoluminescence bands which are associated with the recombination of the S2QA- and S2QB charge pairs, respectively, exhibited parallel decay courses during photoinhibitory treatment. Similarly, the amplitudes of the flash-induced delayed luminescence components ascribed to the recombination of S20A and S2OB charge pairs and having half life-times of about 3 s and 30 s, respectively, declined in parallel with the amplitudes of the corresponding Q and B thermoluminescence bands. The course of inhibition of thermoluminescence and delayed luminescence intensity was parallel with that of the rate of oxygen evolution. The peak positions of the B and Q thermoluminescence bands as well as the half life-times of the corresponding delayed luminescence components were not affected by photoinhibition. These results indicate that in isolated thylakoids neither the amount nor the stability of the reduced OB acceptor is preferentially decreased by photoinhibition. We conclude that either the primary target of photodamage is located before the O b binding site in the reaction center of photosystem II or QA and OB undergo simultaneous damage.

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.

Photosystem I-abhängige Phosphorylierung isolierter Chloroplasten mit Ascorbat/2.6-Dichlorphenolindophenol als Elektronendonator und Methylviologen als Elektronenakzeptor / Photosystem I Dependent Phosphorylation of Isolated Chloroplasts with Ascorbate/2,6-Dichlorophenolindophenol as Electron Donor and Methylviologen as Electron Acceptor

1972 ◽  
Vol 27 (4) ◽  
pp. 445-455 ◽  
Author(s):  
Heinrich Strotmann ◽  
Christa Von Gösseln
Keyword(s):  
Electron Transport ◽  
Linear System ◽  
Photosystem I ◽  
Electron Acceptor ◽  
Electron Flow ◽  
Phosphorylation Site ◽  
Cyclic System ◽  
Atp Production ◽  
Proton Uptake ◽  
Isolated Chloroplasts

Photosystem I related phosphorylation of isolated chloroplasts was investigated with special reference to the stoichiometry between ATP production and electron transprt (ATP: 2e⊖). The system studied contained DCMU to inhibit electron flow from photosystem II, ascorbate and DPIP to supply electrons to photosystem I, and methylviologen as electron acceptor. The following results were obtained:1. Basal electron transport is stimulated by the addition of the phosphorylating system, indicating that phosphorylation is really coupled to non-cyclic electron flow. The ratio ATP: 2e⊖ is 1, when the increase of electron flow obtained by the addition of ADP and phosphate is correlated to phosphorylation. This ratio is constant upon varying several parameters including DPIP concentration and light intensity.2. In the absence of methylviologen a DPIP catalyzed cyclic phosphorylation takes place (cf. I. c.7, 11, 12). Phosphorylation is not increased by the addition of methylviologen, indicating that both, the cyclic DPIP mediated and the non-cyclic system are coupled to the same phosphorylation site and limited by the same reaction step.3. In the absence of oxygen a methylviologen supported cyclic phosphorylation occurs. Comparing optimum rates, phosphorylation under these conditions is about twice as high as in the noncyclic system. Therefore we conclude that two phosphorylation sites are involved in methylviologen catalyzed cyclic electron transport. This system is sensitive against trypsin treatment of the chloroplasts, whereas the linear system is not.4. The two cyclic systems as well as the non-cyclic system are coupled to reversible proton uptake. Furthermore the linear system exhibits an irreversible uptake of hydrogen ions, which is stoichiometric to electron flow. From the reversible and the irreversible components of the pH changes the ratio of the proton pump to electron transprt can be calculated. Under steady state conditions the ration H⨁ : e⊖ approaches 1.

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.

Different kinetics of photoinactivation of photosystem I-mediated electron transport and P700 in isolated thylakoid membranes

2003 ◽  
Vol 69 (1) ◽  
pp. 41-48 ◽  
Author(s):  
Maya Velitchkova ◽  
Inmaculada Yruela ◽  
Miguel Alfonso ◽  
Pablo J. Alonso ◽  
Rafael Picorel
Keyword(s):  
Electron Transport ◽  
Photosystem I ◽  
Thylakoid Membranes ◽  
Kinetics Of
Sign in / Sign up

Export Citation Format

Share Document