On the Role of Plastoquinone in Photosynthesis

1971 ◽  
Vol 26 (4) ◽  
pp. 341-352 ◽  
Author(s):  
H. Böhme ◽  
S. Reimer ◽  
A. Trebst
Keyword(s):  
Photosystem Ii ◽  
Electron Transport Chain ◽  
Electron Flow ◽  
Cyclic Electron Flow ◽  
Cyclic System ◽  
Transport Chain ◽  
Cyclic Photophosphorylation ◽  
Intact Chloroplasts ◽  
Flow Through

Dibromothymoquinone and its hydroquinone are inhibitors of non cyclic electron flow from water to NADP, anthraquinone or methylviologen. The inhibition is competetively reversed by plastoquinone. It appears that dibromothymoquinone is an antagonist of plastoquinone and that it prevents the enzymic (by the next endogenous carrier of the chloroplast electron transport chain) but not the chemical (by ferricyanide) reoxidation of reduced plastoquinone. This follows from the result that the photoreduction of ferricyanide and DCPIP * is not inhibited by dibromothymoquinone in sonicated chloroplasts and is inhibited in intact chloroplasts to only 60% or 80% respectively. It is concluded that dibromothymoquinone does not inhibit photoreductions by photosystem II.According to their response to dibromothymoquinone, cyclic photophosphorylations can be subdivided in those requiring plastoquinone and those which do not. Menadione catalyzed cyclic photophosphorylation is inhibited by dibromothymoquinone, whereas the PMS catalyzed system is not. The DAD cyclic system is only partly inhibited by dibromothymoquinone. The PMS catalyzed cyclic photophosphorylation in the presence of dibromothymoquinone is antimycin sensitive, which suggests that the PMS system can switch from a plastoquinone dependent system to a plastoquinone independent, but cytochrome b dependent system, which is now antimycin sensitive. Ferredoxin catalyzed cyclic photophosphorylation is inhibited by dibromothymoquinone as well as by antimycin. The data indicate that non cyclic electron flow through both photosystems is obligatory dependent on plastoquinone, whereas cyclic systems do not necessarily include plastoquinone. The relevance of the results to the possibility of different coupling sites in cyclic and non cyclic electron flow systems is discussed.

Site of Action of 2,5-Dimethoxy-3,6-Dichloro-p-Benzoquinone in the Photosynthetic Electron Transport Chain

1981 ◽  
Vol 36 (7-8) ◽  
pp. 656-661 ◽  
Author(s):  
G. Sarojini ◽  
H. Daniell
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Electron Transport Chain ◽  
Electron Transport Rate ◽  
Electron Flow ◽  
Electron Acceptors ◽  
Hill Reaction ◽  
Transport Chain ◽  
Site Of Action ◽  
The Hill

Abstract Electron Acceptors, Photosystem II, Quinones and Quinonediamines Dichlorodimethoxy-/?-benzoquinone (DCDMQ) was tested for its site of action in the photo­ synthetic electron transport chain. Hill reaction mediated by DCDMQ was insensitive to DBMIB (1 nm) but sensitive to DCMU, suggesting its site of action before plastoquinone but after Q -the primary electron acceptor of photosystem II. Extraction of freeze-dried chloroplasts with heptane and analyzing their capacity to photo-oxidize water using various Hill oxidants revealed that silicomolybdate (SiMO) and DCDMQ could effectively restore the activity. Diaminodurene (DAD) in the presence of ferricyanide could restore 40% of the activity. But ferricyanide alone failed to restore the ability to photo-oxidize water in heptane extracted chloroplasts. Similarly, N a2S 0 3 which is known to cause a bottleneck in the electron flow at plastoquinone affected the ferricyanide Hill reaction. Hill reactions mediated by SiMO and DCDMQ were insensitive to the addition of Na2SO3, suggesting that both these oxidants intercept electrons before plastoquinone. But 50% of the activity was lost when sulfite was added to the Hill reaction mediated by DADox. DNP-INT, melittin and picrylhydrazyl were recently introduced as photosystem II inhibitors inhibiting the electron flow between Q and the PQ pool. While DCBQ and DCDMQ Hill reactions were insensitive to DNP-INT, ferricyanide was highly sensitive. The quinonediamines TMPD and DADox showed 50% decrease in the electron transport rate, similar to heptane extracted or sulfite inhibited chloroplasts. Melittin increased the electron transport rate when ferricyanide or TMPD was the Hill oxidant, while DCBQ and DCDMQ reduction remained unaffected. However, DADox Hill reaction showed 50% inhibition in the presence of melittin. Picrylhydrazyl - which inhibits the electron flow between Q and the PQ pool - inhibited the Hill reaction of all the PS II electron acceptors except that of DCDMQ. It is possible that there is another site of intercepting electrons between Q and plastoquinone before the site where most of the quinonediamines accept electrons.

Physiological Role of Cyclic Electron Flow in Higher Plants

2012 ◽  
Vol 30 (1) ◽  
pp. 100
Author(s):  
Wei HUANG ◽  
Shi-Bao ZHANG ◽  
Kun-Fang CAO
Keyword(s):  
Higher Plants ◽  
Electron Flow ◽  
Physiological Role ◽  
Cyclic Electron Flow

scholarly journals The Role of Selected Wavelengths of Light in the Activity of Photosystem II in Gloeobacter violaceus

2021 ◽  
Vol 22 (8) ◽  
pp. 4021
Author(s):  
Monika Kula-Maximenko ◽  
Kamil Jan Zieliński ◽  
Ireneusz Ślesak
Keyword(s):  
Photosystem Ii ◽  
Spectral Composition ◽  
Photosynthetic Electron Transport ◽  
Metabolic Energy ◽  
Light Conditions ◽  
Gloeobacter Violaceus ◽  
Transport Chain ◽  
Cyanobacterial Culture ◽  
Photosynthetic Antennas

Gloeobacter violaceus is a cyanobacteria species with a lack of thylakoids, while photosynthetic antennas, i.e., phycobilisomes (PBSs), photosystem II (PSII), and I (PSI), are located in the cytoplasmic membrane. We verified the hypothesis that blue–red (BR) light supplemented with a far-red (FR), ultraviolet A (UVA), and green (G) light can affect the photosynthetic electron transport chain in PSII and explain the differences in the growth of the G. violaceus culture. The cyanobacteria were cultured under different light conditions. The largest increase in G. violaceus biomass was observed only under BR + FR and BR + G light. Moreover, the shape of the G. violaceus cells was modified by the spectrum with the addition of G light. Furthermore, it was found that both the spectral composition of light and age of the cyanobacterial culture affect the different content of phycobiliproteins in the photosynthetic antennas (PBS). Most likely, in cells grown under light conditions with the addition of FR and G light, the average antenna size increased due to the inactivation of some reaction centers in PSII. Moreover, the role of PSI and gloeorhodopsin as supplementary sources of metabolic energy in the G. violaceus growth is discussed.

scholarly journals An overview of chagasic cardiomyopathy: pathogenic importance of oxidative stress

2005 ◽  
Vol 77 (4) ◽  
pp. 695-715 ◽  
Author(s):  
Michele A. Zacks ◽  
Jian-Jun Wen ◽  
Galina Vyatkina ◽  
Vandanajay Bhatia ◽  
Nisha Garg
Keyword(s):  
Oxidative Stress ◽  
Electron Transport Chain ◽  
Common Source ◽  
Oxygen Species ◽  
Pathogen Invasion ◽  
Immune Mediated ◽  
Transport Chain ◽  
Chagasic Cardiomyopathy ◽  
The Common

There is growing evidence to suggest that chagasic myocardia are exposed to sustained oxidative stress-induced injuries that may contribute to disease progression. Pathogen invasion- and replication-mediated cellular injuries and immune-mediated cytotoxic reactions are the common source of reactive oxygen species (ROS) in infectious etiologies. However, our understanding of the source and role of oxidative stress in chagasic cardiomyopathy (CCM) remains incomplete. In this review, we discuss the evidence for increased oxidative stress in chagasic disease, with emphasis on mitochondrial abnormalities, electron transport chain dysfunction and its role in sustaining oxidative stress in myocardium. We discuss the literature reporting the consequences of sustained oxidative stress in CCM pathogenesis.

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 Purification of Helicobacter pylori NCTC 11637 Cytochrome bc1 and Respiration with d-Proline as a Substrate

2009 ◽  
Vol 192 (5) ◽  
pp. 1410-1415 ◽  
Author(s):  
Minoru Tanigawa ◽  
Tomomitsu Shinohara ◽  
Katsushi Nishimura ◽  
Kumiko Nagata ◽  
Morio Ishizuka ◽  
...  
Keyword(s):  
Helicobacter Pylori ◽  
Amino Acid ◽  
Electron Transport ◽  
Electron Transport Chain ◽  
Electron Flow ◽  
Gene Clusters ◽  
Acid Dehydrogenase ◽  
Amino Acid Dehydrogenase ◽  
Transport Chain ◽  
H Pylori

ABSTRACT Helicobacter pylori is a microaerophilic bacterium associated with gastric inflammation and peptic ulcers. Knowledge of how pathogenic organisms produce energy is important from a therapeutic point of view. We found d-amino acid dehydrogenase-mediated electron transport from d-proline or d-alanine to oxygen via the respiratory chain in H. pylori. Coupling of the electron transport to ATP synthesis was confirmed by using uncoupler reagents. We reconstituted the electron transport chain to demonstrate the electron flow from the d-amino acids to oxygen using the recombinant cytochrome bc 1 complex, cytochrome c-553, and the terminal oxidase cytochrome cbb 3 complex. Upon addition of the recombinant d-amino acid dehydrogenase and d-proline or d-alanine to the reconstituted electron transport system, reduction of cytochrome cbb 3 and oxygen consumption was revealed spectrophotometrically and polarographically, respectively. Among the constituents of H. pylori's electron transport chain, only the cytochrome bc 1 complex had been remained unpurified. Therefore, we cloned and sequenced the H. pylori NCTC 11637 cytochrome bc 1 gene clusters encoding Rieske Fe-S protein, cytochrome b, and cytochrome c 1, with calculated molecular masses of 18 kDa, 47 kDa, and 32 kDa, respectively, and purified the recombinant monomeric protein complex with a molecular mass of 110 kDa by gel filtration. The absorption spectrum of the recombinant cytochrome bc 1 complex showed an α peak at 561 nm with a shoulder at 552 nm.

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