History and Function: The Respiratory and Photosynthetic Electron Transport Chains

Author(s):  
Peter Nicholls
2020 ◽  
Vol 22 (1) ◽  
pp. 342
Author(s):  
Ginga Shimakawa ◽  
Ayaka Kohara ◽  
Chikahiro Miyake

In eukaryotic algae, respiratory O2 uptake is enhanced after illumination, which is called light-enhanced respiration (LER). It is likely stimulated by an increase in respiratory substrates produced during photosynthetic CO2 assimilation and function in keeping the metabolic and redox homeostasis in the light in eukaryotic cells, based on the interactions among the cytosol, chloroplasts, and mitochondria. Here, we first characterize LER in photosynthetic prokaryote cyanobacteria, in which respiration and photosynthesis share their metabolisms and electron transport chains in one cell. From the physiological analysis, the cyanobacterium Synechocystis sp. PCC 6803 performs LER, similar to eukaryotic algae, which shows a capacity comparable to the net photosynthetic O2 evolution rate. Although the respiratory and photosynthetic electron transports share the interchain, LER was uncoupled from photosynthetic electron transport. Mutant analyses demonstrated that LER is motivated by the substrates directly provided by photosynthetic CO2 assimilation, but not by glycogen. Further, the light-dependent activation of LER was observed even with exogenously added glucose, implying a regulatory mechanism for LER in addition to the substrate amounts. Finally, we discuss the physiological significance of the large capacity of LER in cyanobacteria and eukaryotic algae compared to those in plants that normally show less LER.


1970 ◽  
Vol 44 (3) ◽  
pp. 540-546 ◽  
Author(s):  
R. P. Levine ◽  
A. Paszewski

Photosynthetic electron transport is markedly affected in mixotrophic cells of ac-20 because they lack the capacity to form the wild-type level of cytochrome 559, as well as Q, the quencher of fluorescence of photochemical system II. The other components of the electron-transport chain, as well as reactions dependent upon photochemical system I, are unaffected in the mutant strain. These observations are discussed in terms of the previously reported effects of the ac-20 mutation on CO2 fixation and ribulose-1,5-diphosphate carboxylase activity.


1988 ◽  
Vol 43 (7-8) ◽  
pp. 581-588 ◽  
Author(s):  
Bernhard Dietz ◽  
Iris Moors ◽  
Ute Flammersfeld ◽  
Wolfgang Rühle ◽  
Aloysius Wild

The investigations described here were carried out in the context of our research project on the physiological, biochemical, and cytomorphological characterization of spruce trees growing in natural habitats and showing damage of varying intensity. Here we report on specific aspects of the photosynthetic apparatus. The aim of the measurements was to analyze whether or not the activity of the photosynthetic electron transport pathway is affected in damaged trees. The investigations were carried out on a 20 to 25-year-old spruce plantation in the Hunsrück mountains and on an 80-year-old spruce plantation in the Westerwald mountains. The photosynthetic electron transport rate was determined by photoreduction of 2,6-dichlorophenolindophenol. A decrease of the electron transport rate was shown in the damaged spruce trees in comparison to the apparently healthy trees. The investigation of the water splitting enzyme system - determined in the Hillreaction by feeding in electrons by means of diphenylcarbazide - indicates that the electron transport on the oxidizing side of photosystem II is impaired. The results imply that the photosynthetic electron transport chains in the thylakoid membranes of the spruce chloroplasts are sites of early injurious effects. This is in agreement with the electron microscopic analyses which show consistently that early damage occurs especially at the cellular membranes. This membrane damage is apparent even in the green needles of damaged spruce trees.


Several plastoquinones with different or modified side chains have been characterized in plant material: they are localized in the inner thylakoid membrane of the chloroplast. So far only plastoquinone-45 (PQ-45) has been identified as an obligatory functional component of the photosynthetic electron transport chain in chloroplasts between photosystem II and photosystem I. A special form (semiquinone) of PQ-45 acts as primary acceptor Q of photosystem II, a large pool of PQ-45 as electron buffer, interconnecting several electron transport chains. The rôle of PQ, in energy conservation (ATP formation) is of particular current interest. Owing to vectorial electron flow across the thylakoid membrane, plastoquinone is thought to be reduced on the outside and plastohydroquinone to be oxidized on the inside of the membrane. This results in a proton translocation across the membrane and a build-up of a proton motive force which drives ATP formation. Old and new plastoquinone antagonists are described and the relevance of inhibitor studies on the rôle of plastoquinone in electron flow and photophosphorylation is discussed. Open questions and current problems of the mechanism of plastoquinone/plastoquinol transport across the membrane - and of proton translocation connected to it - relevant for the mechanism of energy conservation in photosynthesis, are pointed out.


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