Structure, Carbon Dioxide Fixation and Metabolism of Stomata

1974 ◽  
Vol 1 (2) ◽  
pp. 221 ◽  
Author(s):  
CJ Pearson ◽  
FL Milthorpe

Studies were made of the structure and rates of CO2 fixation of epidermis and of changes in organic metabolites in Commelina cyanea during transition to light and dark in both normal and CO2-free air. Guard cells of C. cyanea and Vicia faba contain numerous highly developed mitochondria and starch-forming chloroplasts (mitochondria: chloroplast ratios of 3 : 1) in comparison to other epidermal cells with few mitochondria and rudimentary plastids without starch. Their rates of photosynthesis per chloroplast appeared to be at least as high as those of the mesophyll, but circumstantial evidence suggested that about half of current photosynthate was respired. The rate of CO2 fixation in the dark was about 0.2–0.4% of that in the light. Illumination caused an increase, and darkening a decrease, of aperture, malate, and organic acid 1% within the epidermis of C. cyanea. Darkening in CO2-free air was accompanied by only slight decreases in aperture and malate. There were close positive correlations between aperture and concentration of malate and between aperture and organic acid 14C. During opening, the rise in organic acid 14C was associated with a decline in amino acid 14C. It is suggested that organic acids may be formed through aspartate and possibly also from sugars and other amino acids entering the tricarboxylic acid cycle. Concentrations of sugars were not related to aperture although they increased on illumination and declined about 2 h after darkening. Polysaccharide concentrations in the epidermis of darkened leaves were similar to those in illuminated leaves.

2021 ◽  
Author(s):  
E-Bin Gao ◽  
Penglin Ye ◽  
Haiyan Qiu ◽  
Junhua Wu ◽  
Huayou Chen

Abstract Background: The outstanding ability of directly assimilating carbon dioxide and sunlight to produce biofuels and chemicals impels photosynthetic cyanobacteria to become attractive organisms for the solution to the global warming crises and the world energy growth. The cyanobacteria-based method for ethanol production has been increasingly regarded as alternatives to food biomass-based fermentation and traditional petroleum-based production. Therefore, we engineered the model cyanobacterium Synechocystis sp. PCC 6803 to synthesize ethanol and optimized the biosynthetic pathways for improving ethanol production under photoautotrophic conditions.Results: In this study, we successfully achieved the photosynthetic production of ethanol from atmospheric carbon dioxide by an engineered mutant Synechocystis sp. PCC 6803 with over-expressing the heterologous genes encoding Zymomonas mobilis pyruvate decarboxylase (PDC) and Escherichia coli NADPH-dependent alcohol dehydrogenase (YqhD). The engineered strain was further optimized by an alternative engineering approach to improve cell growth, and increase the intracellular supply of the precursor pyruvate for ethanol production under photoautotrophic conditions. This approach includes blocking phosphoenolpyruvate synthetic pathway from pyruvate, removing glycogen storage, and shunting carbon metabolic flux of tricarboxylic acid cycle. Through redirecting and optimizing the metabolic carbon flux of Synechocystis, a high ethanol-producing efficiency was achieved (248 mg L-1 day-1) under photoautotrophic conditions with atmospheric CO2 as the sole carbon source. Conclusions: The engineered strain SYN009 (∆slr0301/pdc-yqhD, ∆slr1176/maeB) would become a valuable biosystem for photosynthetic production of ethanol and for expanding our knowledge of exploiting cyanobacteria to produce value chemicals directly from atmospheric CO2.


1968 ◽  
Vol 110 (2) ◽  
pp. 313-335 ◽  
Author(s):  
D. F. Heath

A scheme is presented that shows how the reactions involved in gluconeogenesis, glycolysis and the tricarboxylic acid cycle are linked in rat liver. Equations are developed that show how label is redistributed in aspartate, glutamate and phosphopyruvate when it is introduced as specifically labelled pyruvate or glucose either at a constant rate (steady-state theory) or at a variable rate (non-steady-state theory). For steady-state theory the fractions of label introduced as specifically labelled pyruvate that are incorporated into glucose and carbon dioxide are also given, and for both theories the specific radioactivities of aspartate and glutamate relative to the specific radioactivity of the substrate. The theories allow for entry of label into the tricarboxylic acid cycle via both oxaloacetate and acetyl-CoA, for 14CO2 fixation and for loss of label from the tricarboxylic acid cycle in glutamate, but not for losses in citrate. They also allow for incomplete symmetrization of label in oxaloacetate due to incomplete equilibration with fumarate both in the extramitochondrial part of the cell and in the mitochondrion on entry of oxaloacetate into the tricarboxylic acid cycle. In the latter case failure both of oxaloacetate to equilibrate with malate and of malate to equilibrate with fumarate are considered.


Award of Medals 1961 The Copley Medal is awarded to Sir Hans Krebs, F.R.S. Sir Hans Krebs has made outstanding contributions to knowledge of the chemical pathways of metabolism. In 1932, with Henseleit, he used tissue slices to demonstrate the synthesis of urea and found that additions of ornithine stimulated the process. Ornithine was regarded as uniting with carbon dioxide and ammonia to give arginine, with citrulline as an intermediate. The enzyme arginase liberated urea and a molecule of ornithine, so that the process could begin again. Subsequent research has shown that the postulated cycle is essentially valid, although more detail has been introduced; carbamyl phosphate, argininosuccinate and adenosine triphosphate have been brought in and aspartic acid has replaced ammonia in the reaction with citrulline. The more complicated version owes much to the fundamental work initiated by Krebs in 1937 on the tricarboxylic acid cycle. This process is now seen as the main route for oxidizing the two-carbon fragment produced in the biological degradation of carbohydrates, fatty acids and arninoacids.


1964 ◽  
Vol 42 (6) ◽  
pp. 883-888 ◽  
Author(s):  
S. Suryanarayanan ◽  
W. B. McConnell

When uredospores of Puccinia graminis var. tritici (race 15B) were incubated at pH 6.2 in phosphate buffer containing either acetate-1-C14or -2-C14, about 12% of the radioactivity was removed from the solution in a period of 3 hours. Respired carbon dioxide contained about 45% and 22% of the carbon-14 taken up as acetate-1-C14and acetate-2-C14, respectively. Incorporation of carbon-14 into spore components was considerably higher with acetate-2-C14than with acetate-1-C14. With either tracer most of the radioactivity in water-soluble spore materials was accounted for in amino acids and neutral substances. Glutamic acid was particularly radioactive and accounted for about 40% of the radioactivity in the amino acid fraction. Incorporation of carbon-14 into the glutamic acid skeleton was consistent with the view that both the tricarboxylic acid cycle and the glyoxalate cycle were functioning.


1981 ◽  
Vol 194 (3) ◽  
pp. 867-875 ◽  
Author(s):  
E M Nuutinen ◽  
K J Peuhkurinen ◽  
E P Pietiläinen ◽  
J K Hiltunen ◽  
I E Hassinen

1. The contribution of Co2 fixation to the anaplerotic mechanisms in the myocardium was investigated in isolated perfused rat hearts. 2. K+-induced arrest of the heart was used to elicit a transition in the concentrations of the intermediates of the tricarboxylic acid cycle. 3. Incorporation of 14C from [14]bicarbonate into tricarboxylic acid-cycle intermediates was measured and the rates of the reactions of the cycle were estimated by means of a linear optimization program which solves the differential equations describing a simulation model of the tricarboxylic acid cycle and related reactions. 4. The results showed that the rate of CO2 fixation is dependent on the metabolic state of the myocardium. Upon a sudden diminution of cellular ATP consumption, the pool size of the tricarboxylic acid-cycle metabolites increased and the rate of label incorporation from [14C]bicarbonate into the cycle metabolites increased simultaneously. The computer model was necessary to separate the rapid equilibration between bicarbonate and some metabolites from the potentially anaplerotic reactions. The main route of anaplerosis during metabolite accumulation was through malate + oxaloacetate. Under steady-state conditions there was a constant net outward flow from the tricarboxylic acid cycle via the malate + oxaloacetate pool, with a concomitant anaplerotic flow from metabolites forming succinyl-CoA (3-carboxypropionyl-CoA).


1967 ◽  
Vol 105 (1) ◽  
pp. 323-331 ◽  
Author(s):  
D. S. Cameron ◽  
E. A. Cossins

1. The pathway of ethanol metabolism in cotyledons of 3-day-old pea seedlings has been examined by incubating tissue slices with [1−14C]ethanol and [2−14C]ethanol for periods up to 1hr. 2. Ethanol was rapidly incorporated into citrate and glutamate but relatively small amounts of 14C were present in the evolved carbon dioxide even after 1hr. of ethanol metabolism. 3. Similar data were obtained from experiments in which [1,2−14C2]acetaldehyde and [14C]acetate were supplied. 4. The results are interpreted as indicating that ethanol is metabolized essentially via the reactions of the tricarboxylic acid cycle with a substantial drain of α-oxoglutarate to support the biosynthesis of glutamate. 5. It is concluded that oxaloacetate, required for the incorporation of ethanol into citrate, arises mainly from the transamination of aspartate and the fixation of carbon dioxide.


1969 ◽  
Vol 15 (1) ◽  
pp. 57-60 ◽  
Author(s):  
Victor F. Lachica ◽  
Paul A. Hartman

The stimulatory effect of acetyl-CoA and the inhibitory effect by L-aspartate and some intermediates of the tricarboxylic acid cycle in the assimilation of CO2 by crude extracts of group D streptococci suggest that the pyruvate carboxylase of Streptococcus faecium and the phosphoenolpyruvate carboxylase of S. bovis are allosteric enzymes. This implies that these enzymes are sites for the control of the amount of aspartate and of the tricarboxylic acid cycle intermediates synthesized.


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