Indoleacetic acid stimulation of phosphorylation and bicarbonate fixation by chloroplast preparations in light

1972 ◽  
Vol 50 (7) ◽  
pp. 1523-1527 ◽  
Author(s):  
Imre A. Tamàs ◽  
Brian D. Atkins ◽  
Susette M. Ware ◽  
R. G. S. Bidwell
Keyword(s):  
Electron Transport ◽  
Indoleacetic Acid ◽  
Atp Synthesis ◽  
Swiss Chard ◽  
Bicarbonate Fixation ◽  
Acetabularia Mediterranea ◽  
Degree Of Coupling ◽  
Phosphorylation Rate ◽  
Stimulation Of

The rate of phosphorylation in illuminated chloroplast preparations from spinach, Swiss chard, or Acetabularia mediterranea was increased by physiological concentrations of indoleacetic acid (IAA), optimum effect being obtained at 10−7 M. Treated chloroplasts gave an increased P/2e ratio, suggesting a greater degree of coupling between electron transport and ATP synthesis. Five minutes after incubation the effect of the hormone was already noticeable. During prolonged illumination the effect of IAA was greatly magnified, raising the phosphorylation rate more than threefold over the control rate. Stimulation of 14C-bicarbonate fixation was also observed in the presence of the same levels of IAA.

An investigation into the influence of IAA and malate on in vivo and in vitro rates of dark carbon dioxide fixation in coleoptile tissue

1977 ◽  
Vol 55 (12) ◽  
pp. 1641-1645 ◽  
Author(s):  
I. J. Dymock ◽  
B. Hill ◽  
A. W. Bown
Keyword(s):  
Carbon Dioxide ◽  
Avena Sativa ◽  
Indoleacetic Acid ◽  
Enzymic Activity ◽  
Time Period ◽  
Rapid Effect ◽  
Bicarbonate Fixation ◽  
Stimulation Of

Etiolated Avena sativa L. cv. Victory coleoptiles were used to determine the influence of indoleacetic acid (IAA) or malate on in vivo and in vitro rates of CO2 fixation. In addition, the influence of malate on IAA-stimulated growth was investigated. Concentrations of malate which stimulate growth did not influence the in vivo rate of dark [14C]bicarbonate fixation but did inhibit in vitro phosphoenolpyruvate carboxylase (EC 4.1.1.31) activity. IAA did not influence this enzymic activity or reduce the inhibition of the enzyme by malate, and the rate of [14C]bicarbonate fixation was not measurably influenced by 20 μM IAA within the time period required for IAA stimulation of growth to become apparent. In the absence of atmospheric levels of CO2, 1 mM malate and 20 μM IAA stimulate growth in a weakly synergistic manner. These results are discussed in relationship to a suggestion that IAA-stimulated H+ secretion and growth involves a rapid effect on CO2 fixation.

Effect of Magnesium and Calcium Ions on the Photoelectron Transport Activity of Low-Salt Suspended Hydrilla verticillata Thylakoids: Possible Sites of Cation Interaction

1998 ◽  
Vol 53 (9-10) ◽  
pp. 849-856
Author(s):  
Sujata R. Mishra ◽  
Surendra Chandra Sabat
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Electron Donor ◽  
Water Oxidation ◽  
Electron Flow ◽  
Hydrilla Verticillata ◽  
Transport Activity ◽  
Low Salt ◽  
Electron Transport Activity ◽  
Stimulation Of

Stimulatory effect of divalent cations like calcium (Ca2+) and magnesium (Mg2+) was investigated on electron transport activity of divalent cation deficient low-salt suspended (LS) thylakoid preparation from a submerged aquatic angiosperm, Hydrilla verticillata. Both the cations stimulated electron transport activity of LS-suspended thylakoids having an intact water oxidation complex. But in hydroxylamine (NH2OH) - or alkaline Tris - washed thylakoid preparations (with the water oxidation enzyme impaired), only Ca2+ dependent stimulation of electron transport activity was found. The apparent Km of Ca2+ dependent stimulation of electron flow from H2O (endogenous) or from artificial electron donor (exogenous) to dichlorophenol indophenol (acceptor) was found to be identical. Calcium supported stimulation of electron transport activity in NH2OH - or Tris - washed thylakoids was electron donor selective, i.e., Ca2+ ion was only effective in electron flow with diphenylcarbazide but not with NH2OH as electron donor to photosystem II. A magnesium effect was observed in thylakoids having an intact water oxidation complex and the ion became unacceptable in NH2OH - or Tris - washed thylakoids. Indirect experimental evidences have been presented to suggest that Mg2+ interacts with the water oxidation complex, while the Ca2+ interaction is localized betw een Yz and reaction center of photosystem II.

Electron Transport and Coupled Energy Generation in Pseudomonas saccharophila

1971 ◽  
Vol 49 (11) ◽  
pp. 1175-1182 ◽  
Author(s):  
M. Ishaque ◽  
A. Donawa ◽  
M. I. H. Aleem
Keyword(s):  
Oxygen Consumption ◽  
Electron Transport ◽  
Cytochrome C ◽  
Atp Synthesis ◽  
Succinate Oxidation ◽  
Atp Formation ◽  
Low Concentrations ◽  
Oxidase Enzyme ◽  
Succinate Oxidase ◽  
Pseudomonas Saccharophila

The respiratory chain system of heterotrophically grown Pseudomonas saccharophila contained cytochromes of the b, c, a, and o types and also the NADH and succinate oxidase enzyme systems. Cell-free extracts catalyzed phosphorylation coupled to the oxidation of NADH, succinate, and ascorbate (plus cytochrome c). The P/O ratios were in the range of 1.00 for generated NADH, 0.29 for added NADH, 0.50 for succinate, and 0.25 for ascorbate (plus cytochrome c).The oxidative phosphorylation was uncoupled by 2,4-dinitrophenol, 2,6-dibromophenol, pentachlorophenol, m-chlorocarbonyl cyanide phenylhydrazone, and dicumarol without any inhibition of oxygen consumption. Phosphorylation coupled to NADH oxidation was completely inhibited by the flavoprotein inhibitors such as rotenone, amytal, and atabrine; these inhibitors had no effect, however, on the ATP synthesis associated with succinate oxidation. Antimycin A or 2-n-nonyl-4-hydroxyquinoline-N-oxide as well as cyanide or azide at low concentrations completely inhibited the phosphate esterification coupled to the oxidation of NADH or succinate, but had little or no effect on the oxygen consumption. Relatively higher concentrations of oligomycin were required for a complete inhibition of the electron-transport-linked ATP formation.

scholarly journals Alpha Carbonic Anhydrase 5 Mediates Stimulation of ATP Synthesis by Bicarbonate in Isolated Arabidopsis Thylakoids

2021 ◽  
Vol 12 ◽  
Author(s):  
Tatiana P. Fedorchuk ◽  
Inga A. Kireeva ◽  
Vera K. Opanasenko ◽  
Vasily V. Terentyev ◽  
Natalia N. Rudenko ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Arabidopsis Thaliana ◽  
Carbonic Anhydrase ◽  
Atp Synthesis ◽  
Thylakoid Membranes ◽  
Wild Type ◽  
Gene Encoding ◽  
Mutant Lines ◽  
Stimulation Of ◽  
Soluble Carbonic Anhydrase

We studied bicarbonate-induced stimulation of photophosphorylation in thylakoids isolated from leaves of Arabidopsis thaliana plants. This stimulation was not observed in thylakoids of wild-type in the presence of mafenide, a soluble carbonic anhydrase inhibitor, and was absent in thylakoids of two mutant lines lacking the gene encoding alpha carbonic anhydrase 5 (αCA5). Using mass spectrometry, we revealed the presence of αCA5 in stromal thylakoid membranes of wild-type plants. A possible mechanism of the photophosphorylation stimulation by bicarbonate that involves αCA5 is proposed.

Inhibition of oxygen evolution by ivalin

1994 ◽  
Vol 72 (2) ◽  
pp. 177-181 ◽  
Author(s):  
Ernesto Bernal-Morales ◽  
Alfonso Romo De Vivar ◽  
Bertha Sanchez ◽  
Martha Aguilar ◽  
Blas Lotina-Hennsen
Keyword(s):  
Electron Transport ◽  
Photosystem Ii ◽  
Sesquiterpene Lactone ◽  
Oxygen Evolution ◽  
Electron Flow ◽  
Atp Synthesis ◽  
Naturally Occurring ◽  
Transport Inhibitor ◽  
Proton Uptake ◽  
Key Words Oxygen

The inhibition of ATP synthesis, proton uptake, and electron transport (basal, phosphorylating, and uncoupled) from water to methylviologen by ivalin (a naturally occurring sesquiterpene lactone in Zaluzania triloba and Iva microcephala) indicates that it acts as electron transport inhibitor. Since photosystem I and electron transport from DPC to QA were not affected, while the electron flow of uncoupled photosystem II from H2O to DAD and from water to silicomolybdate was inhibited, we concluded that the site of inhibition of ivalin is located at the oxygen evolution level. Key words: oxygen evolution, ivalin, photosynthesis, sesquiterpene lactone.

scholarly journals A comparison of the effects of NN′-dicyclohexylcarbodi-imide, oligomycin A and aurovertin on energy-linked reactions in mitochondria and submitochondrial particles

1968 ◽  
Vol 108 (3) ◽  
pp. 445-456 ◽  
Author(s):  
A. M. Roberton ◽  
Caroline T. Holloway ◽  
I G Knight ◽  
R B Beechey
Keyword(s):  
Potent Inhibitor ◽  
Atp Synthesis ◽  
Mitochondrial Fraction ◽  
Optimum Concentration ◽  
Submitochondrial Particles ◽  
Nicotinamide Nucleotide Transhydrogenase ◽  
Oligomycin A ◽  
Submitochondrial Particle ◽  
Site Of Action ◽  
Stimulation Of

1. The effects of dicyclohexylcarbodi-imide, oligomycin A and aurovertin on enzyme systems related to respiratory-chain phosphorylation were compared. Dicyclohexylcarbodi-imide and oligomycin A have very similar functional effects, giving 50% inhibition of ATP-utilizing and ATP-generating systems at concentrations below 0·8nmole/mg. of submitochondrial-particle protein. Aurovertin is a more potent inhibitor of ATP synthesis, giving 50% inhibition at 0·2nmole/mg. of protein. However, aurovertin is a less potent inhibitor of ATP-utilizing systems: the ATP-driven energy-linked nicotinamide nucleotide transhydrogenase is 50% inhibited at 3·0nmoles/mg. of protein and the ATP-driven reduction of NAD+ by succinate is 50% inhibited at 0·95nmole/mg. of protein. 2. With EDTA-particles (prepared by subjecting mitochondria to ultrasonic radiation at pH9 in the presence of 2mm-EDTA) the maximum stimulation of the ATP-driven partial reactions is effected by similar concentrations of oligomycin A and dicylcohexylcarbodi-imide, but the latter is less effective. The stimulatory effects of suboptimum concentrations of dicyclohexylcarbodi-imide and oligomycin A are additive. Aurovertin does not stimulate these reactions or interfere with the stimulation by the other inhibitors. 3. Dicyclohexylcarbodi-imide and oligomycin A stimulate the aerobic energy-linked nicotinamide nucleotide transhydrogenase of EDTA-particles, but the optimum concentration is higher than that required for the ATP-driven partial reactions. Aurovertin has no effect on this reaction. 4. The site of action of dicyclohexylcarbodi-imide is in CF0, the mitochondrial fraction that confers oligomycin sensitivity on F1 mitochondrial adenosine triphosphatase.

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