scholarly journals Carbon dioxide fixation by Calvin-Cycle enzymes improves ethanol yield in yeast

2013 ◽  
Vol 6 (1) ◽  
pp. 125 ◽  
Author(s):  
Víctor Guadalupe-Medina ◽  
H Wisselink ◽  
Marijke AH Luttik ◽  
Erik de Hulster ◽  
Jean-Marc Daran ◽  
...  
2018 ◽  
Vol 11 (1) ◽  
Author(s):  
Ioannis Papapetridis ◽  
Maaike Goudriaan ◽  
María Vázquez Vitali ◽  
Nikita A. de Keijzer ◽  
Marcel van den Broek ◽  
...  

1966 ◽  
Vol 101 (3) ◽  
pp. 642-646 ◽  
Author(s):  
CW Baldry ◽  
DA Walker ◽  
C Bucke

1. Induction periods in carbon dioxide fixation by isolated pea chloroplasts were shortened by small quantities of Calvin-cycle intermediates. The additional fixation was larger than that which would have followed direct stoicheiometric conversion into ribulose 1,5-diphosphate. 2. When chloroplasts were illuminated in the absence of added substrates (other than carbon dioxide) soluble products were formed in the medium that stimulated fixation by fresh chloroplasts. 3. The induction periods were lengthened by washing the chloroplasts. Addition of catalytic quantities of Calvin-cycle intermediates then decreased the induction periods to their previous values. 4. The induction period was extended by a decrease in temperature but was largely unaffected by a decrease in light-intensity that was sufficient to decrease the maximum rate. 5. It is concluded that the lag periods are a consequence of the loss of Calvin-cycle intermediates, such as sugar phosphates, through the intact chloroplast envelope and that these losses can be made good by new synthesis from carbon dioxide in the reactions of the Calvin cycle.


2018 ◽  
Author(s):  
Ciaran McFarlane ◽  
Nita R. Shah ◽  
Burak V. Kabasakal ◽  
Charles A.R. Cotton ◽  
Doryen Bubeck ◽  
...  

AbstractIn plants, carbon dioxide is fixed via the Calvin cycle in a tightly regulated process. Key to this regulation is the conditionally disordered protein CP12. CP12 forms a complex with two Calvin cycle enzymes, glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase (PRK), inhibiting their activities. The mode of CP12 action was unknown. By solving crystal structures of CP12 bound to GAPDH, and the ternary GAPDH-CP12-PRK complex by electron cryo-microscopy, we reveal that formation of the N-terminal disulfide pre-orders CP12 prior to binding the PRK active site. We find that CP12 binding to GAPDH influences substrate accessibility of all GAPDH active sites in the binary and ternary inhibited complexes. Our model explains how CP12 integrates responses from both redox state and nicotinamide dinucleotide availability to regulate carbon fixation.One Sentence SummaryHow plants turn off carbon fixation in the dark.


1947 ◽  
Vol 170 (2) ◽  
pp. 461-465
Author(s):  
Santiago Grisolia ◽  
Birgit Vennesland

1949 ◽  
Vol 180 (1) ◽  
pp. 299-305 ◽  
Author(s):  
Donald B. Melville ◽  
John G. Pierce ◽  
C.W.H. Partridge

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