scholarly journals Factors Affecting Light Induced Fixation of Carbon Dioxide by Isolated Spinach Chloroplasts.

1959 ◽  
Vol 34 (3) ◽  
pp. 318-323 ◽  
Author(s):  
Martin Gibbs ◽  
Nona Calo
1998 ◽  
Vol 118 (1) ◽  
pp. 31-40 ◽  
Author(s):  
Brian R. Eggins ◽  
Peter K.J. Robertson ◽  
Eileen P. Murphy ◽  
Elaine Woods ◽  
John T.S. Irvine

1968 ◽  
Vol 46 (12) ◽  
pp. 1475-1478 ◽  
Author(s):  
John R. Vose ◽  
Mary Spencer

A 60–70% inhibition of spinach chloroplast PMS1-catalyzed cyclic photophosphorylation was observed following a 5-min pre-incubation in the dark with either 0.25 mM phloridzin or 10 μM quinacrine. Phloridzin was also shown to severely inhibit the endogenous synthesis of ATP (no catalyst being present). The inhibitors had only a slight effect on the fixation of carbon dioxide. Addition of 3-phosphoglyceric acid was found to inhibit the fixation of CO2 while ribose 5-phosphate stimulated CO2 fixation, even in the presence of 0.25 mM phloridzin.


2019 ◽  
Author(s):  
Javier Oller ◽  
David A. Sáez ◽  
Esteban Vöhringer-Martinez

<div><div><div><p>Local reactivity descriptors such as atom condensed Fukui functions are promising computational tools to study chemical reactivity at specific sites within a molecule. Their applications have been mainly focused on isolated molecules in their most stable conformation without considering the effects of the surroundings. Here, we propose to combine QM/MM Born-Oppenheimer molecular dynamics simulations to obtain the microstates (configurations) of a molecular system using different representations of the molecular environment and calculate Boltzmann weighted atom condensed local reac- tivity descriptors based on conceptual DFT. Our approach takes the conformational fluctuations of the molecular system and the polarization of its electron density by the environment into account allowing us to analyze the effect of changes in the molecular environment on reactivity. In this contribution, we apply the method mentioned above to the catalytic fixation of carbon dioxide by crotonyl-CoA carboxylase/reductase and study if the enzyme alters the reactivity of its substrate compared to an aqueous solution. Our main result is that the protein en- vironment activates the substrate by the elimination of solute-solvent hydrogen bonds from aqueous solution in the two elementary steps of the reaction mechanism: the nucleophilic attack of a hydride anion from NADPH on the α, β unsaturated thioester and the electrophilic attack of carbon dioxide on the formed enolate species.</p></div></div></div>


1941 ◽  
Vol 139 (1) ◽  
pp. 483-484
Author(s):  
H.G. Wood ◽  
C.H. Werkman ◽  
Allan Hemingway ◽  
A.O. Nier

1947 ◽  
Vol 171 (1) ◽  
pp. 445-446 ◽  
Author(s):  
Birgit Vennesland ◽  
Joseph Ceithaml ◽  
Miriam C. Gollub

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