Answer:
Carbon dioxide + water + energy from light produces glucose and oxygen.
so B
I believe the answer is b
Answer:
ΔG'° for the coupled reaction = -16.7 kJ/mol
<em>Note: The question is missing some parts. The complete question is as follows:</em>
<em>The first reaction in glycolysis is the phosphorylation of glucose:
</em>
<em>
Pi+glucose⟶glucose−6−phosphate+H2O
</em>
<em>This is a thermodynamically unfavorable process, with ΔG∘′= +13.8kJ/mol. In a liver cell at 37 ∘C the concentrations of both phosphate and glucose are normally maintained at about 5 mM each.</em>
<em>This very low concentration of the desired product would be unfavorable for glycolysis. In fact the reaction is coupled to ATP hydrolysis to give the overall reaction: ATP + glucose → glucose-6-phosphate + ADP + H+</em>
<em>What is the ΔG'° for the coupled reaction?</em>
Explanation:
The coupling of ATP hydrolysis which is a thermodynamically favourable reaction to the phosphorylation of glucose makes it favourable. Since the two reactions constitute a sequential reaction, their standard free energy changes are additive.
For ATP hydrolysis: ATP + H₂O ---> ADP + Pi ; ΔG'° = -30.5KJ/mol
For phosphorylation of glucose: Pi + glucose⟶glucose−6−phosphate + H2O ; ΔG'° = +13.8 kJ/Mol
For the overall reaction: ATP + glucose → glucose-6-phosphate + ADP + H⁺ ; ΔG'° = 13.8 + (-30.5) kJ/mol = -16.7 kJ/mol
Therefore, ΔG'° for the coupled reaction = -16.7 kJ/mol
Answer:
Changes in the surface features of an area affect can many factors.
Explanation:
For example, they can affect precipitation, temperature, and even winds. Large grids can also make it difficult for meteorologists to accurately predict small-scale weather events.
When an allosteric enzyme is directly affected by a molecule that is not its substrate, this effect on the enzyme is called a heterotropic effect.
<h3>What is an allosteric enzyme?</h3>
Allosteric enzymes are catalysts that exhibit a site for binding that is distinct from the active site.
Allosteric enzymes are controlled by many effector compounds that can bind to different sites.
The active site of the enzyme is the molecular domain of this protein where reactants can bind during a chemical reaction.
The heterotropic effects occur when the ligands of allosteric modulators (effectors) are linked to the enzyme.
An allosteric modulator is a molecule that binds to the enzyme in a site different to the active site and this binding alters its tridimensional conformation, thereby activating it or deactivating it.
In conclusion, when an allosteric enzyme is directly affected by a molecule that is not its substrate, this effect on the enzyme is called a heterotropic effect.
Learn more about allosteric enzymes here:
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