Explain Why Rubisco Is A Key Component In Photosynthesis
Question 2
a.)
Rubisco is a key component in photosynthesis. It is an enzyme involved in the fixation of atmospheric carbon dioxide.
b.)
Due to global warming, the increased temperature can influence Rubisco which can catalyses oxygenation over carboxylation. During carboxylation CO2 is fixed and raised temperature enhancing oxygenation.
c.)
Level of PGA depends on Rubisco with who is going to bind. Rubisco is an enzyme that reacts with CO2 and O2. The reaction with O2 competes with carboxylation reaction where CO2 is fixed. That means, if Rubisco catalyses with O2, the oxygenase wins, if there is enough CO2 in atmosphere, like at the beginning of evolution then it is the carboxylation reaction.
d.)
Increased oxygenase and reduced carboxylate activity will slow down the photosynthesis. Oxygenation is waste full process because 3-phosphoglycerate is created at reduced rate and higher metabolic cost compared with Rubiscone carboxylase activity.
e.) …show more content…
According to article, Rubisco have tendency to aggregate when large subunits are isolated.
They bind together when their identical hydrophobic or the same charged regions are closely revealed to the environment.
Aggregation in vintro can be successfully altered with the help of RbcX chaperone which is able to bind to partly folded large-subunit chain and interact with small subunits. Study by Liu at all. reveals, that aggregation in vintro helped them to obtain 40% of active Rubisco and allowed them to study the effects of mutation in order to get a better enzyme.
Protein aggregation in vintro, does not include the complex of cellular environment, which is very important and crucial in protein aggregation.
(114 words)
f.)
Rubisco from cyanobacteria and plants is a multimeric protein consisting of eight distinct subunits bound to eight structural small subunits.
g.)
Chaperons are proteins which help polypeptides fold correctly. If protein is miss fold chaperons help them to recover and refold.
Chaperons also combat protein aggregation by binding to temporarily exposed, interactive surfaces of individual protein at the beginning of formation or folding.
Chaperonin, the member of chaperons’ family has a more specific function. It is present in plants, animals and bacteria. Chaperonin is forming a cavity where individual misfolded polypeptide is placed and polypeptide chain has opportunity to complete his folding into monomers away from others. This process also need ATP and it is for opening and closing those cavities.
Bacteria Escherichia coli contain chaperonin GroEL/ES is effectively forms active Rubisco from cyanobacteria in vintro. However, it can not form from unfolded subunit.
h.)
Genetic manipulation can create the more effective Rubisco. The mutation of large subunit would improve catalytic properties which are dependent on them. If it would be possible to increase carboxylase activity or decrease O2 inhibition it would improve plant productivity.
a.)
Rubisco is a key component in photosynthesis. It is an enzyme involved in the fixation of atmospheric carbon dioxide.
b.)
Due to global warming, the increased temperature can influence Rubisco which can catalyses oxygenation over carboxylation. During carboxylation CO2 is fixed and raised temperature enhancing oxygenation.
c.)
Level of PGA depends on Rubisco with who is going to bind. Rubisco is an enzyme that reacts with CO2 and O2. The reaction with O2 competes with carboxylation reaction where CO2 is fixed. That means, if Rubisco catalyses with O2, the oxygenase wins, if there is enough CO2 in atmosphere, like at the beginning of evolution then it is the carboxylation reaction.
d.)
Increased oxygenase and reduced carboxylate activity will slow down the photosynthesis. Oxygenation is waste full process because 3-phosphoglycerate is created at reduced rate and higher metabolic cost compared with Rubiscone carboxylase activity.
e.) …show more content…
According to article, Rubisco have tendency to aggregate when large subunits are isolated.
They bind together when their identical hydrophobic or the same charged regions are closely revealed to the environment.
Aggregation in vintro can be successfully altered with the help of RbcX chaperone which is able to bind to partly folded large-subunit chain and interact with small subunits. Study by Liu at all. reveals, that aggregation in vintro helped them to obtain 40% of active Rubisco and allowed them to study the effects of mutation in order to get a better enzyme.
Protein aggregation in vintro, does not include the complex of cellular environment, which is very important and crucial in protein aggregation.
(114 words)
f.)
Rubisco from cyanobacteria and plants is a multimeric protein consisting of eight distinct subunits bound to eight structural small subunits.
g.)
Chaperons are proteins which help polypeptides fold correctly. If protein is miss fold chaperons help them to recover and refold.
Chaperons also combat protein aggregation by binding to temporarily exposed, interactive surfaces of individual protein at the beginning of formation or folding.
Chaperonin, the member of chaperons’ family has a more specific function. It is present in plants, animals and bacteria. Chaperonin is forming a cavity where individual misfolded polypeptide is placed and polypeptide chain has opportunity to complete his folding into monomers away from others. This process also need ATP and it is for opening and closing those cavities.
Bacteria Escherichia coli contain chaperonin GroEL/ES is effectively forms active Rubisco from cyanobacteria in vintro. However, it can not form from unfolded subunit.
h.)
Genetic manipulation can create the more effective Rubisco. The mutation of large subunit would improve catalytic properties which are dependent on them. If it would be possible to increase carboxylase activity or decrease O2 inhibition it would improve plant productivity.