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Bioc 2061: Bioenergetics
Tutorial 9: Photosynthesis #2
The enzyme consists of 8 large subunits and 8 small subunits. The large subunits contain the
active site of the enzyme.
Enzyme is inactive because ribulose 1, 5-bisphosphate is bound to the active site. This results
in the closed conformation which makes the lysine side chain for carbamylation inaccessible.
Activation is catalyzed by rubisco activase by promoting the ATP-dependent release of the
ribulose 1,5-bisphosphate and the lysine side chain is exposed for carbamylation.
Activation requires light, CO2, Mg2+ and correct stromal pH.
A non-substrate CO2 adds to the ε-amino group of lysine 201 to form a carbamate.
Mg2+ binds to the negatively charged carbamate and is linked to rubisco via an oxygen in the
carbamate on Lys201 and two in the carboxyl groups of Glu204 and Asp203
The enzyme is now active.
Ribulose 1, 5-bisphosphate binds to Mg2+ through its keto group and an adjacent hydroxyl
group.
This complex is readily deprotonated to form an enediolate intermediate.
The intermediate reacts with a CO2 to form 2-carboxy-3-keto-D-arabinitol 1,5- bisphosphate.
A molecule of H2O is then added to this β- ketoacid to form an intermediate that cleaves to
form two molecules of 3-phosphoglycerate.
3. The Reduction and the Regeneration stages in the Calvin (Benson -Basshum) Cycle.
It is no specific for CO2 only. During evolution, O2 levels were lower and there was no
selective pressure to discriminate between CO 2 and O2.
Oxygen competes with CO2 at the active site.
About once in every three or four turnovers, rubisco catalyzes the condensation of O 2 with
ribulose 1,5-bisphosphate.
This reaction forms 3-phosphoglycerate and 2-phosphoglycolate. The 2-phosphoglycolate is
metabolically useless.
Hence the full name of the enzyme is ribulose 1,5-bisphosphate carboxylase/oxygenase.
This oxygenase is energetically demanding on the cell as carbons have to be salvaged from 2-
phosphoglycolate via photorespiration.
6. C3 and C4 plants overcome the oxygenase activity by photorespiration and increasing the
concentration of CO2 in photosynthetic cells, respectively.
C4 plants: C4 pathway
CO2 Fixation and Rubisco Activity Are Spatially Separated.
Involves mesophyll and bundle sheath cells.
In the mesophyll cell, CO2 is condensed with phosphoenolpyruvate to form
oxaloacetate in a reaction catalyzed by phosphoenolpyruvate carboxylase.
Phosphoenolpyruvate carboxylase has a lower Km for CO 2 and, hence, higher
affinity than Rubisco.
O2 is a poor substrate for this enzyme, there even at low concentrations of CO 2, CO2 is
still fixed.
In some species, oxaloacetate is converted into malate or aspartate by an NADP +-
malic enzyme(
Malate/aspartate enters the bundle-sheath cell and is oxidatively-decarboxylated
within the chloroplasts by an NADP+-malic enzyme
The released CO2 enters the Calvin cycle in the usual way by condensing with
ribulose 1,5-bisphosphate.
Pyruvate formed in this decarboxylation reaction returns to the mesophyll cell.
phosphoenolpyruvate is formed from pyruvate by pyruvate-Pi dikinase.
7. C3 plants reassimilate the nitrogen lost at glycine decarboxylase by Nitrogen Fixation via the
GS/GOGAT pathway.
The glutamine synthetase (GS) fixes ammonium on a glutamate molecule to form glutamine.
This glutamine reacts subsequently with 2-oxoglutarate to form two molecules of glutamate,
this step being catalysed by the glutamine 2-oxoglutarate amino transferase (or glutamate
synthase, GOGAT)
α-Ketoglutarate, undergoes reductive amination with glutamine to produce glutamate
8. In CAM plants, CO2 Capture and Rubisco Action Are Temporally Separated