In your body, what process converts the chemical energy found in glucose into the chemical energy found in ATP?


cellular respiration..... This is the name given to the process by which the body converts food energy to energy stored in ATP.

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Energy is observed in two basic forms: potential and kinetic. Which of the following correctly matches these forms with a source of energy?


The process of cellular respiration, which converts simple sugars such as glucose into CO2 and water, is an example of _____.


Which of the following statements about the combustion of glucose with oxygen to form water and carbon dioxide (C6H12O6 + 6 O2 → 6 CO2 + 6 H2O) is correct?


The entropy of the products is greater than the entropy of the reactants. note: A large molecule (glucose) has been converted into several smaller molecules (water and carbon dioxide); thus, the products have more disorder (greater entropy) than the reactants.


Select the highest energy form of adenosine from the following images. Adenosine triphosphate (ATP) is the high-energy form of adenosine because it contains the most phosphate groups (three). This molecule fuels many different endergonic (energy-requiring) enzymatic processes in biological organisms. ATP molecules diffuse or are transported to the place where the energy is needed and deliver chemical energy from the breaking of their phosphate bonds.


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In this reaction _____.


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In this reaction _____.


heat has been released to the environment. note: The potential energy of the products is less than that of the reactants.


exergonic note: The energy released by an exergonic reaction can be used to drive an endergonic reaction.


It is acquired by a reactant in an endergonic reaction. note: by acquiring the phosphate group the reactant acquires energy.


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This graph illustrates a(n) _____ reaction.


Select the INCORRECT association. enzyme ... proteinexergonic ... uphillexergonic ... spontaneouspotential energy ... positional energykinetic energy ... motion


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The cycling between ATP and ADP + Pi provides an energy coupling between catabolic and anabolic pathways.


Consider a situation in which the enzyme is operating at optimum temperature and pH, and has been saturated with substrate. What is your best option for increasing the rate of the reaction?


Increase the enzyme concentration If an enzyme is saturated with substrate, and it is operating at optimum pH and optimum temperature, there is very little that can be done except to increase the enzyme concentration. Some enzymes can be activated further by allosteric activators, in which case one might add some activator to the reaction. But otherwise, increasing the enzyme concentration is the only option.


Competitive inhibitors compete physically and structurally with the substrate for an enzyme’s active site; they can be outcompeted by adding extra substrate. Noncompetitive inhibitors do not compete for the active site, but inhibit the enzyme by binding elsewhere and changing the enzyme’s shape. Irreversible inhibitors bind directly to the active site by covalent bonds, which change the structure of the enzyme and inactivate it permanently. Most medications are enzyme inhibitors of one kind or another.


You have added an irreversible inhibitor to a sample of enzyme and substrate. At this point, the reaction has stopped completely.What can you do to regain the activity of the enzyme?


You have an enzymatic reaction proceeding at the optimum pH and optimum temperature. You add a competitive inhibitor to the reaction and notice that the reaction slows down.What can you do to speed the reaction up again?


Add more substrate; it will outcompete the inhibitor and increase the reaction rate.Competitive inhibition can be overcome by adding more substrate to outcompete the inhibitor. Many drugs used to treat different medical conditions, including hypertension, are competitive inhibitors. It is fairly easy to make a molecule that is similar in structure to a particular substrate because the known enzyme’s shape can be used as a model of what the molecule needs to look like. It is more difficult to make a noncompetitive inhibitor because it is less obvious what the noncompetitive inhibitor’s shape and structure should be.


The Haber process is typically carried out at a temperature of approximately 500∘C. What would happen to the rate of the forward reaction if the temperature were lowered to 100∘C?


The reaction rate would decrease. Most reactions double in rate for each 10∘C increase in temperature.


What would happen to the rate of the forward reaction if the concentration of nitrogen were decreased?


The reaction rate would decrease. As the concentration of nitrogen decreases, collisions between nitrogen and hydrogen are less likely to occur.


increasing the concentration of ammonia. The concentration of NH3 affects how quickly N2 and H2 can be made.


Both forward and reverse rates increase. The Haber process can be cheaply catalyzed using porous iron. A much more effective catalyst for the Haber process is osmium; however, it is very expensive and toxic.

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Rank these by reaction rate, as measured by the rate of product formation per unit time, from lowest reaction rate to highest reaction rate. To rank items as equivalent, overlap them.