Reaction Kinetics - Physical Chemistry
Card 1 of 84
Which of the following is true regarding competitive inhibition?
I. They form covalent bonds with the active site
II. They are reversible
III. They are similar to allosteric inhibitors
Which of the following is true regarding competitive inhibition?
I. They form covalent bonds with the active site
II. They are reversible
III. They are similar to allosteric inhibitors
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Competitive inhibition decreases enzyme activity by binding to the active site of the enzyme. Recall that active sites are sites on enzymes where the substrates bind. Upon binding to the enzyme, the substrates undergo changes that facilitate and speed up the chemical reaction. A competitive inhibitor binds to this active site and prevents the substrate from binding. With no binding, the substrate will not undergo the necessary changes and, subsequently, the chemical reaction. A key characterisitic of competitive inhibitors is that the bond between the inhibitor and the active site is reversible. This means that the chemical bonds involved here are weak, reversible noncovalent bonds such as hydrogen bonds and van der Waals forces. Covalent bonds are very strong and are usually found in irreversible interactions.
Allosteric inhibitors are molecules that bind to enzymes at their allosteric site(s). In this way, the allosteric inhibiton is very similar to, and is a subset of, another type of enzyme inhibition, noncompetitive inhibition.
Competitive inhibition decreases enzyme activity by binding to the active site of the enzyme. Recall that active sites are sites on enzymes where the substrates bind. Upon binding to the enzyme, the substrates undergo changes that facilitate and speed up the chemical reaction. A competitive inhibitor binds to this active site and prevents the substrate from binding. With no binding, the substrate will not undergo the necessary changes and, subsequently, the chemical reaction. A key characterisitic of competitive inhibitors is that the bond between the inhibitor and the active site is reversible. This means that the chemical bonds involved here are weak, reversible noncovalent bonds such as hydrogen bonds and van der Waals forces. Covalent bonds are very strong and are usually found in irreversible interactions.
Allosteric inhibitors are molecules that bind to enzymes at their allosteric site(s). In this way, the allosteric inhibiton is very similar to, and is a subset of, another type of enzyme inhibition, noncompetitive inhibition.
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Which of the following is true regarding noncompetitive inhibitors?
I. They do not form covalent bonds with the active site
II. They alter both Km and Vmax
III. They alter the shape of the active site
Which of the following is true regarding noncompetitive inhibitors?
I. They do not form covalent bonds with the active site
II. They alter both Km and Vmax
III. They alter the shape of the active site
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Noncompetitive inhibitors bind to enzymes and prevent the formation of the enzyme-substrate complex. These inhibitors bind to a location other than the active site. Upon binding, the inhibitors alter the conformation of the active site and prevent the binding of substrate. They form covalent bonds with the enzyme; therefore, these are irreversible inhibitors and are hard to remove. 
and 
are altered by both types of inhibitors (competitive and noncompetitive). Competitive inhibitors alter the 
whereas the noncompetitive inhibitors alter the 
.
This implies that competitive inhibition can be overcome by increasing substrate concentration whereas noncompetitive inhibition cannot. Molecularly this makes sense. Competitive inhibitors bind reversibly to the active site and prevent binding of substrate. If we were to drastically increase its concentration, substrate will compete with and remove the competitive inhibitor from the active site. Noncompetitive inhibitors, on the other hand, alter the conformation of the active site, making it hard for substrates to bind to the active site; therefore, the substrate will not be able bind, regardless of the substrate concentration.
Noncompetitive inhibitors bind to enzymes and prevent the formation of the enzyme-substrate complex. These inhibitors bind to a location other than the active site. Upon binding, the inhibitors alter the conformation of the active site and prevent the binding of substrate. They form covalent bonds with the enzyme; therefore, these are irreversible inhibitors and are hard to remove.
This implies that competitive inhibition can be overcome by increasing substrate concentration whereas noncompetitive inhibition cannot. Molecularly this makes sense. Competitive inhibitors bind reversibly to the active site and prevent binding of substrate. If we were to drastically increase its concentration, substrate will compete with and remove the competitive inhibitor from the active site. Noncompetitive inhibitors, on the other hand, alter the conformation of the active site, making it hard for substrates to bind to the active site; therefore, the substrate will not be able bind, regardless of the substrate concentration.
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A researcher is analyzing the effects of an unknown inhibitor. He observes that the inhibition can be overcome by increasing the concentration of the substrate. What can you conclude about this inhibitor?
A researcher is analyzing the effects of an unknown inhibitor. He observes that the inhibition can be overcome by increasing the concentration of the substrate. What can you conclude about this inhibitor?
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Recall that competitive inhibition can be overcome by increasing substrate concentration. Competitive inhibitors alter the Michaelis constant, 
, but maintain the 
(maximum reaction rate). Inhibitors act to decrease the reaction rate. To figure out the effect of competitive inhibitors on the Michaelis constant, we need to look at the Michaelis-Menten equation.
where 
is reaction rate, 
is maximum reaction rate, 
is substrate concentration, and 
is the Michaelis constant. Since reaction rate is inversely proportional to the 
, competitive inhibitors will increase 
and, thereby, decrease reaction rate.
Recall that competitive inhibition can be overcome by increasing substrate concentration. Competitive inhibitors alter the Michaelis constant,
where
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The slope of a Lineweaver-Burk plot is 
and the x-intercept is 
. Upon addition of a noncompetitive inhibitor the slope increases to 
. Which of the following is the correct value of 
(Michaelis constant) after the addition of the inhibitor?
The slope of a Lineweaver-Burk plot is
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To answer this question we need to first figure out the equation for slope and x-intercept of Lineweaver-Burk plot. The Linweaver-Burk plot is a graphical way to plot the Michaelis-Menten equation. It is defined as the reciprocal of Michaelis-Menten equation. Michaelis-Menten equation is as follows.
where 
is reaction rate, 
is maximum reaction rate, 
is substrate concentration, and 
is the Michaelis constant. Taking the reciprocal of this gives us
The slope, therefore, is 
. The x-intercept can be found by plugging in zero for the Y value (the reaction rate, 
). The x-intercept is 
.
The question states that the slope is 
and the x-intercept is 
. Using the equation for x-intercept we can solve for 
.
Using the equation for slope we can solve for 
Recall that the addition of a noncompetitive inhibitor alters the 
but not the 
; therefore, 
is still 
after the addition of noncompetitive inhibitior.
Note that if we were asked to solve for the 
, we would have had to use the new slope (
) and the same 
value (
).
To answer this question we need to first figure out the equation for slope and x-intercept of Lineweaver-Burk plot. The Linweaver-Burk plot is a graphical way to plot the Michaelis-Menten equation. It is defined as the reciprocal of Michaelis-Menten equation. Michaelis-Menten equation is as follows.
where
The slope, therefore, is
The question states that the slope is
Using the equation for slope we can solve for
Recall that the addition of a noncompetitive inhibitor alters the
Note that if we were asked to solve for the
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Upon addition of an inhibitor, which of the following is expected to happen in a catalytic reaction?
Upon addition of an inhibitor, which of the following is expected to happen in a catalytic reaction?
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Inhibitors are molecules that prevent the action of catalysts. They bind to catalysts and prevent substrate binding, thereby halting the catalytic action. Since catalysts increase the speed of a reaction, addition of an inhibitor will lower the speed of the reaction. This does not mean that the reaction will stop proceeding; it simple means that it will take longer for the reaction to complete (reach equilibrium).
Remember that a catalyst speeds up both the forward and the reverse reaction; therefore, inhibitors will slow down both reactions. As mentioned, inhibitors will only slow down the reaction. The amount of products produced (equilibrium) will not change, although it will take longer for products to form.
Inhibitors are molecules that prevent the action of catalysts. They bind to catalysts and prevent substrate binding, thereby halting the catalytic action. Since catalysts increase the speed of a reaction, addition of an inhibitor will lower the speed of the reaction. This does not mean that the reaction will stop proceeding; it simple means that it will take longer for the reaction to complete (reach equilibrium).
Remember that a catalyst speeds up both the forward and the reverse reaction; therefore, inhibitors will slow down both reactions. As mentioned, inhibitors will only slow down the reaction. The amount of products produced (equilibrium) will not change, although it will take longer for products to form.
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inhibitors bind to the active site and inhibitors alter the binding affinity of substrate and catalyst.
inhibitors bind to the active site and inhibitors alter the binding affinity of substrate and catalyst.
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There are two main types of inhibitors. Competitive inhibitors bind to the active site of the catalyst and prevent substrate from binding. This phenomenon causes a decreasing in the binding affinity of substrate and catalyst. However, competitive inhibitors can be overcome by adding excess substrates. The substrates will dissociate the competitive inhibitor and carry out the reaction; therefore, the reaction can still be carried out at a faster rate and the maximum rate of reaction is not altered.
Noncompetitive inhibitors bind to the catalyst at an allosteric site. They alter the conformation of the active site and prevent substrate binding. They cannot be overcome by addition of excess substrate; therefore, they lower the maximum rate of reaction.
There are two main types of inhibitors. Competitive inhibitors bind to the active site of the catalyst and prevent substrate from binding. This phenomenon causes a decreasing in the binding affinity of substrate and catalyst. However, competitive inhibitors can be overcome by adding excess substrates. The substrates will dissociate the competitive inhibitor and carry out the reaction; therefore, the reaction can still be carried out at a faster rate and the maximum rate of reaction is not altered.
Noncompetitive inhibitors bind to the catalyst at an allosteric site. They alter the conformation of the active site and prevent substrate binding. They cannot be overcome by addition of excess substrate; therefore, they lower the maximum rate of reaction.
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Which of the following is true regarding the Michaelis constant?
Which of the following is true regarding the Michaelis constant?
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Michaelis constant, or 
, is defined as the concentration of substrate at which the reaction rate is half the maximum (
). It is a useful measure of how much substrate is needed for reaction to proceed rapidly. A reaction with a high Michaelis constant will need lots of substrate to reach high reaction rates whereas a reaction with low Michaelis constant will need small amounts of substrate to reach high reaction rates.
Michaelis constant, or
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Which of the following will have the greatest increase in reaction rate?
Which of the following will have the greatest increase in reaction rate?
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Reaction rate, according to Michaelis-Menten model is as follows.
where 
is reaction rate, 
is maximum reaction rate, 
is substrate concentration, and 
is the Michaelis constant. If we analyze the given options, we will observe that the greatest increase in 
occurs when 
is doubled (increased by a factor of 2). Increasing substrate concentration by a factor of 2 will have nearly the same effect; however, since 
is also found in the denominator it will only slightly contribute to an increase in 
.
Note that the units for 
is molarity, 
is molarity, and 
is 
. Solving for 
will give us units of 
.
Reaction rate, according to Michaelis-Menten model is as follows.
where
Note that the units for
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Consider the following reaction parameters.
Substrate concentration = 
Michaelis constant = 
What can you conclude about the reaction rate?
Consider the following reaction parameters.
Substrate concentration =
Michaelis constant =
What can you conclude about the reaction rate?
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To solve this problem we need to use the Michaelis-Menten equation.
where 
is reaction rate, 
is maximum reaction rate, 
is substrate concentration, and 
is the Michaelis constant. If we plug in the given values we get a reaction rate of
Note that the Michaelis-Menten equation implies that the 
will never exceed 
. Regardless of how high the substrate concentration is, the reaction rate will approach 
but will never equal or exceed it. You can try this by substituting very high values for substrate concentration. The 
will get very close to 0.2 (
) but will never equal or exceed it.
To solve this problem we need to use the Michaelis-Menten equation.
where
Note that the Michaelis-Menten equation implies that the
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The Michaelis-Menten model implies that the Michaelis constant will the reaction rate.
The Michaelis-Menten model implies that the Michaelis constant will the reaction rate.
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The Michaelis-Menten equation is as follows.
Where 
is reaction rate, 
is maximum reaction rate, 
is substrate concentration, and 
is the Michaelis constant. Since the Michaelis constant, 
, is in the denominator, the reaction rate is inversely proportional to the Michaelis constant; therefore, increasing the Michaelis constant will decrease the reaction rate.
The Michaelis-Menten equation is as follows.
Where
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Which of the following is true regarding competitive inhibition?
I. They form covalent bonds with the active site
II. They are reversible
III. They are similar to allosteric inhibitors
Which of the following is true regarding competitive inhibition?
I. They form covalent bonds with the active site
II. They are reversible
III. They are similar to allosteric inhibitors
Tap to reveal answer
Competitive inhibition decreases enzyme activity by binding to the active site of the enzyme. Recall that active sites are sites on enzymes where the substrates bind. Upon binding to the enzyme, the substrates undergo changes that facilitate and speed up the chemical reaction. A competitive inhibitor binds to this active site and prevents the substrate from binding. With no binding, the substrate will not undergo the necessary changes and, subsequently, the chemical reaction. A key characterisitic of competitive inhibitors is that the bond between the inhibitor and the active site is reversible. This means that the chemical bonds involved here are weak, reversible noncovalent bonds such as hydrogen bonds and van der Waals forces. Covalent bonds are very strong and are usually found in irreversible interactions.
Allosteric inhibitors are molecules that bind to enzymes at their allosteric site(s). In this way, the allosteric inhibiton is very similar to, and is a subset of, another type of enzyme inhibition, noncompetitive inhibition.
Competitive inhibition decreases enzyme activity by binding to the active site of the enzyme. Recall that active sites are sites on enzymes where the substrates bind. Upon binding to the enzyme, the substrates undergo changes that facilitate and speed up the chemical reaction. A competitive inhibitor binds to this active site and prevents the substrate from binding. With no binding, the substrate will not undergo the necessary changes and, subsequently, the chemical reaction. A key characterisitic of competitive inhibitors is that the bond between the inhibitor and the active site is reversible. This means that the chemical bonds involved here are weak, reversible noncovalent bonds such as hydrogen bonds and van der Waals forces. Covalent bonds are very strong and are usually found in irreversible interactions.
Allosteric inhibitors are molecules that bind to enzymes at their allosteric site(s). In this way, the allosteric inhibiton is very similar to, and is a subset of, another type of enzyme inhibition, noncompetitive inhibition.
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Which of the following is true regarding noncompetitive inhibitors?
I. They do not form covalent bonds with the active site
II. They alter both Km and Vmax
III. They alter the shape of the active site
Which of the following is true regarding noncompetitive inhibitors?
I. They do not form covalent bonds with the active site
II. They alter both Km and Vmax
III. They alter the shape of the active site
Tap to reveal answer
Noncompetitive inhibitors bind to enzymes and prevent the formation of the enzyme-substrate complex. These inhibitors bind to a location other than the active site. Upon binding, the inhibitors alter the conformation of the active site and prevent the binding of substrate. They form covalent bonds with the enzyme; therefore, these are irreversible inhibitors and are hard to remove. and are altered by both types of inhibitors (competitive and noncompetitive). Competitive inhibitors alter the whereas the noncompetitive inhibitors alter the .
This implies that competitive inhibition can be overcome by increasing substrate concentration whereas noncompetitive inhibition cannot. Molecularly this makes sense. Competitive inhibitors bind reversibly to the active site and prevent binding of substrate. If we were to drastically increase its concentration, substrate will compete with and remove the competitive inhibitor from the active site. Noncompetitive inhibitors, on the other hand, alter the conformation of the active site, making it hard for substrates to bind to the active site; therefore, the substrate will not be able bind, regardless of the substrate concentration.
Noncompetitive inhibitors bind to enzymes and prevent the formation of the enzyme-substrate complex. These inhibitors bind to a location other than the active site. Upon binding, the inhibitors alter the conformation of the active site and prevent the binding of substrate. They form covalent bonds with the enzyme; therefore, these are irreversible inhibitors and are hard to remove.
This implies that competitive inhibition can be overcome by increasing substrate concentration whereas noncompetitive inhibition cannot. Molecularly this makes sense. Competitive inhibitors bind reversibly to the active site and prevent binding of substrate. If we were to drastically increase its concentration, substrate will compete with and remove the competitive inhibitor from the active site. Noncompetitive inhibitors, on the other hand, alter the conformation of the active site, making it hard for substrates to bind to the active site; therefore, the substrate will not be able bind, regardless of the substrate concentration.
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A researcher is analyzing the effects of an unknown inhibitor. He observes that the inhibition can be overcome by increasing the concentration of the substrate. What can you conclude about this inhibitor?
A researcher is analyzing the effects of an unknown inhibitor. He observes that the inhibition can be overcome by increasing the concentration of the substrate. What can you conclude about this inhibitor?
Tap to reveal answer
Recall that competitive inhibition can be overcome by increasing substrate concentration. Competitive inhibitors alter the Michaelis constant, , but maintain the (maximum reaction rate). Inhibitors act to decrease the reaction rate. To figure out the effect of competitive inhibitors on the Michaelis constant, we need to look at the Michaelis-Menten equation.
where is reaction rate, is maximum reaction rate, is substrate concentration, and is the Michaelis constant. Since reaction rate is inversely proportional to the , competitive inhibitors will increase and, thereby, decrease reaction rate.
Recall that competitive inhibition can be overcome by increasing substrate concentration. Competitive inhibitors alter the Michaelis constant,
where
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The slope of a Lineweaver-Burk plot is and the x-intercept is . Upon addition of a noncompetitive inhibitor the slope increases to . Which of the following is the correct value of (Michaelis constant) after the addition of the inhibitor?
The slope of a Lineweaver-Burk plot is
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To answer this question we need to first figure out the equation for slope and x-intercept of Lineweaver-Burk plot. The Linweaver-Burk plot is a graphical way to plot the Michaelis-Menten equation. It is defined as the reciprocal of Michaelis-Menten equation. Michaelis-Menten equation is as follows.
where is reaction rate, is maximum reaction rate, is substrate concentration, and is the Michaelis constant. Taking the reciprocal of this gives us
The slope, therefore, is . The x-intercept can be found by plugging in zero for the Y value (the reaction rate, ). The x-intercept is .
The question states that the slope is and the x-intercept is . Using the equation for x-intercept we can solve for .
Using the equation for slope we can solve for
Recall that the addition of a noncompetitive inhibitor alters the but not the ; therefore, is still after the addition of noncompetitive inhibitior.
Note that if we were asked to solve for the , we would have had to use the new slope () and the same value ().
To answer this question we need to first figure out the equation for slope and x-intercept of Lineweaver-Burk plot. The Linweaver-Burk plot is a graphical way to plot the Michaelis-Menten equation. It is defined as the reciprocal of Michaelis-Menten equation. Michaelis-Menten equation is as follows.
where
The slope, therefore, is
The question states that the slope is
Using the equation for slope we can solve for
Recall that the addition of a noncompetitive inhibitor alters the
Note that if we were asked to solve for the
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Upon addition of an inhibitor, which of the following is expected to happen in a catalytic reaction?
Upon addition of an inhibitor, which of the following is expected to happen in a catalytic reaction?
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Inhibitors are molecules that prevent the action of catalysts. They bind to catalysts and prevent substrate binding, thereby halting the catalytic action. Since catalysts increase the speed of a reaction, addition of an inhibitor will lower the speed of the reaction. This does not mean that the reaction will stop proceeding; it simple means that it will take longer for the reaction to complete (reach equilibrium).
Remember that a catalyst speeds up both the forward and the reverse reaction; therefore, inhibitors will slow down both reactions. As mentioned, inhibitors will only slow down the reaction. The amount of products produced (equilibrium) will not change, although it will take longer for products to form.
Inhibitors are molecules that prevent the action of catalysts. They bind to catalysts and prevent substrate binding, thereby halting the catalytic action. Since catalysts increase the speed of a reaction, addition of an inhibitor will lower the speed of the reaction. This does not mean that the reaction will stop proceeding; it simple means that it will take longer for the reaction to complete (reach equilibrium).
Remember that a catalyst speeds up both the forward and the reverse reaction; therefore, inhibitors will slow down both reactions. As mentioned, inhibitors will only slow down the reaction. The amount of products produced (equilibrium) will not change, although it will take longer for products to form.
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inhibitors bind to the active site and inhibitors alter the binding affinity of substrate and catalyst.
inhibitors bind to the active site and inhibitors alter the binding affinity of substrate and catalyst.
Tap to reveal answer
There are two main types of inhibitors. Competitive inhibitors bind to the active site of the catalyst and prevent substrate from binding. This phenomenon causes a decreasing in the binding affinity of substrate and catalyst. However, competitive inhibitors can be overcome by adding excess substrates. The substrates will dissociate the competitive inhibitor and carry out the reaction; therefore, the reaction can still be carried out at a faster rate and the maximum rate of reaction is not altered.
Noncompetitive inhibitors bind to the catalyst at an allosteric site. They alter the conformation of the active site and prevent substrate binding. They cannot be overcome by addition of excess substrate; therefore, they lower the maximum rate of reaction.
There are two main types of inhibitors. Competitive inhibitors bind to the active site of the catalyst and prevent substrate from binding. This phenomenon causes a decreasing in the binding affinity of substrate and catalyst. However, competitive inhibitors can be overcome by adding excess substrates. The substrates will dissociate the competitive inhibitor and carry out the reaction; therefore, the reaction can still be carried out at a faster rate and the maximum rate of reaction is not altered.
Noncompetitive inhibitors bind to the catalyst at an allosteric site. They alter the conformation of the active site and prevent substrate binding. They cannot be overcome by addition of excess substrate; therefore, they lower the maximum rate of reaction.
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Which of the following is always true regarding reaction orders?
Which of the following is always true regarding reaction orders?
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Individual order of reactants is a variable used to determine the rate of a reaction. Each reactant in the rate-limiting step of a reaction is assigned an order (typically zeroth, 1st, or 2nd). The reaction order is the sum of all individual orders. The rate of a reaction is defined as follows.
Where 
is the rate of the reaction, 
and 
are reactants, 
is rate constant, and 
and 
are individual orders. The reaction order of of this reaction would be 
. Note that the rate of a reaction depends on the concentration of reactants, rate constant, and the individual orders. It doesn’t depend on the reaction order.
Individual order of reactants is a variable used to determine the rate of a reaction. Each reactant in the rate-limiting step of a reaction is assigned an order (typically zeroth, 1st, or 2nd). The reaction order is the sum of all individual orders. The rate of a reaction is defined as follows.
Where
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You are analyzing a drug. After performing some tests you observe that the drug elimination follows first order. How long will it take for 75% of drug to be eliminated from the body?
You are analyzing a drug. After performing some tests you observe that the drug elimination follows first order. How long will it take for 75% of drug to be eliminated from the body?
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The half-life is defined as the amount of time it takes to reduce the concentration of a substance (in this case a drug). After one half-life, 50% of the drug will be eliminated and 50% will remain. After the second half-life, half of the remaining drug (25%) will be eliminated; therefore, at the end of second half-life 75% of drug will be eliminated. To solve for this time, we can simply calculate the half-life and multiply it by 2.
To solve this question, we need to know the equation for half-life. It is stated that the reaction follows first-order; therefore, the half-life for a first order reaction is defined as
Where 
is half-life and 
is the rate constant. Since we are not given the rate constant we cannot calculate the half-life.
The half-life is defined as the amount of time it takes to reduce the concentration of a substance (in this case a drug). After one half-life, 50% of the drug will be eliminated and 50% will remain. After the second half-life, half of the remaining drug (25%) will be eliminated; therefore, at the end of second half-life 75% of drug will be eliminated. To solve for this time, we can simply calculate the half-life and multiply it by 2.
To solve this question, we need to know the equation for half-life. It is stated that the reaction follows first-order; therefore, the half-life for a first order reaction is defined as
Where
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Which of the following is true regarding a first order reaction?
Which of the following is true regarding a first order reaction?
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The half-life of a first order reaction is as follows:
Where 
is half-life and 
is the rate constant. The half-life only depends on the rate constant. Since rate constant is in the denominator, half-life and rate constant are inversely proportional. This means that half-life increases as rate constant decreases and vice versa. Concentration of reactants does not affect the half-life for a first order reaction.
The half-life of a first order reaction is as follows:
Where
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The rate constant as temperature increases and as catalyst is added.
The rate constant as temperature increases and as catalyst is added.
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Rate constant is a unique constant for each reaction that determines the rate of a reaction. It is one of several variables that determines the rate of reaction. As rate constant increases the rate of reaction increases. Rate constant depends on two main factors: temperature and activation energy. The rate constant increases as the temperature is increased. Recall that increasing temperature increases the kinetic energy of the molecules; therefore, an increase in temperature will increase the amount of molecules that reach activation energy. This will increase the rate constant and, subsequently, the rate of the reaction.
Rate constant increases as the activation energy is decreased. Activation energy is the energy hill that reactants must overcome to produce products. If the activation energy is decreased then it will be easier for reactants to overcome the energy hill and convert into products; therefore, decreasing activation energy will increase the rate constant and, subsequently, the rate of the reaction. Recall that catalysts speed up a reaction (increase rate of reaction) by lowering activation energy; therefore, catalysts increase the rate constant.
Rate constant is a unique constant for each reaction that determines the rate of a reaction. It is one of several variables that determines the rate of reaction. As rate constant increases the rate of reaction increases. Rate constant depends on two main factors: temperature and activation energy. The rate constant increases as the temperature is increased. Recall that increasing temperature increases the kinetic energy of the molecules; therefore, an increase in temperature will increase the amount of molecules that reach activation energy. This will increase the rate constant and, subsequently, the rate of the reaction.
Rate constant increases as the activation energy is decreased. Activation energy is the energy hill that reactants must overcome to produce products. If the activation energy is decreased then it will be easier for reactants to overcome the energy hill and convert into products; therefore, decreasing activation energy will increase the rate constant and, subsequently, the rate of the reaction. Recall that catalysts speed up a reaction (increase rate of reaction) by lowering activation energy; therefore, catalysts increase the rate constant.
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