Lecture 8 Chapter 6 & 7 Protein Function Enzymes

Question 1

The velocity of a reaction is the quantity of the:
a. reactant that appears in a specified unit of time.
b. product that disappears in a specified unit of time.
c. solution color that disappears in a specified unit of time.
d. reactant that disappears in a specified unit of time.
e. solution color that appears in a specified unit of time.

Answer 1

d. reactant that disappears in a specified unit of time.

Question 2

What is the reaction order if the reaction rate was doubled by doubling the reactant concentration?
a. zero order
b. first order
c. second order
d. pseudo-first order
e. pseudo-second order

Answer 2

b. first order

Question 3

What is the reaction order if the reaction rate was increased by a factor of 4 by doubling the reactant
concentration?
a. zero order
b. first order
c. second order
d. pseudo-first order
e. pseudo-second order

Answer 3

c. second order

Question 4

Which rate equation is TRUE if doubling the concentration of reactant A doubles the reaction rate and
doubling the concentration of reactant B has no effect on the rate?
a. V = k[A]
b. V = k[A][B]
c. V = k[A]2[B]1
d. V = k[A]2[B]
e. V = k[A]2

Answer 4

a. V = k[A]

Question 5

Which statement about pseudo-first order reactions is FALSE?

a. Bimolecular reactions can be pseudo-first-order reactions.

b. The reaction rate will not appear to depend on the concentration of reactant A, whose concentration
greatly exceeds that of reactant B.

c. The reaction has a pseudo-first order if the concentration of one reactant greatly exceeds that of the
second one and if the second reactant is present at low concentrations.

d. The reaction rate will not appear to depend on the concentration of reactant A, whose concentration is significantly less than that of reactant B.

e. Unimolecular reactions cannot be pseudo-first-order reactions.

Answer 5

d. The reaction rate will not appear to depend on the concentration of reactant A, whose concentration is significantly less than that of reactant B.

Question 6

Choose the CORRECT statement concerning the reaction order.
a. First-order rate constants have units M–1 s–1.
b. Biochemical reactions cannot have a zero order.
c. Bimolecular reactions are always second-order reactions.
d. Second-order reactions are usually unimolecular.
e. First-order rate constants have unit s–1.

Answer 6

e. First-order rate constants have unit s–1.

Question 7

Which statement about enzyme kinetics is TRUE?

a. Michaelis–Menten enzymes have sophisticated regulatory properties.

b. The kinetic description of enzymatic activity is required to understand the structure of enzymes.

c. The action of allosteric enzymes increases the metabolic chaos.

d. Allosteric enzymes allow the efficient integration of metabolism.

e. All enzymes obey Michaelis–Menten kinetics.

Answer 7

d. Allosteric enzymes allow the efficient integration of metabolism.

Question 8

Which characteristics are usually the first ones to be determined when studying enzyme activity?
a. Vmax and KM
b. V0 and KM
c. Vmax and V0
d. [S] and KM
e. Vmax and k2

Answer 8

a. Vmax and KM

Question 9

In the Michaelis–Menten model:

a. the reaction equilibrium is attained with time, and the change in the concentration of the product
allows measuring of the reaction rate.

b. a unique characteristic of the enzyme is investigated when the enzyme concentration is relatively
constant and the product formation is negligible.

c. enzyme concentration is relatively constant only near the end of the reaction, so only in the
beginning of the reaction can the velocity be measured precisely.

d. only in the beginning of the reaction, there is no net change in concentrations of S and P, so the
reaction velocity can be measured precisely.

e. the initial velocity depends on [S] only when the entire enzyme is bound to the substrate but the
product has not accumulated yet.

Answer 9

b. a unique characteristic of the enzyme is investigated when the enzyme concentration is relatively
constant and the product formation is negligible.

Question 10

The Michaelis constant:

a. depends on the concentration of the enzyme.

b. displays the maximal rate of the reaction, when it is much less than the substrate concentration.

c. describes the properties of the enzyme.

d. displays the maximal rate of the reaction, when it is equal to the substrate concentration.

e. displays zero-order kinetics, when the it is equal to the substrate concentration.

Answer 10

b. displays the maximal rate of the reaction, when it is much less than the substrate concentration.

Question 11

Which statement about Vmax is TRUE?
a. Vmax is independent of enzyme concentration.
b. For Michaelis–Menten enzymes, the maximal velocity is approached asymptotically.
c. Vmax can be attained only when half of the enzyme is bound to the substrate.
d. The reaction velocity is maximal when the concentration of the substrate equals KM.
e. The reaction velocity is half Vmax when the entire enzyme is bound to the substrate.

Answer 11

b. For Michaelis–Menten enzymes, the maximal velocity is approached asymptotically.

Question 12

What is the consequence of a high KM value of an enzyme?

a. Moderate concentration of the substrate will be enough for maximal enzyme activity.

b. This enzyme has high maximal velocity.

c. The enzyme is present in a large concentration in the cell.

d. High concentration of the substrate should be reached for maximal enzyme activity.

e. The velocity will be directly proportional to the substrate concentration.

Answer 12

d. High concentration of the substrate should be reached for maximal enzyme activity.

Question 13

How can the reciprocal plot of initial velocity NOT be applied?

a. When it is half the maximal speed, the substrate concentration equals KM.

b. It gives a way to define KM when it is plotted against the reciprocal of the substrate concentration.

c. When it is plotted against the reciprocal of the substrate concentration, it allows KM/Vmax to be
defined as a slope of the graph.

d. It allows definition of the reciprocal of the maximal velocity in a double-reciprocal plot.

e. It is part of the Lineweaver–Burk equation.

Answer 13

a. When it is half the maximal speed, the substrate concentration equals KM.

Question 14

How can the turnover number of an enzyme be determined?
a. as Vmax
b. when the enzyme is fully saturated
c. as [E]T
d. when half of the enzyme is occupied with the substrate
e. by the initial velocity

Answer 14

b. when the enzyme is fully saturated

Question 15

Calculate the turnover of an enzyme if the maximal velocity is 0.2 M sec–1 and the product concentration
after the reaction is 1 M.
a. 0.2 sec
b. 0.2 sec–1
c. 5 sec
d. 0.5 sec
e. 0.5 sec–1

Answer 15

b. 0.2 sec–1

Question 16

An enzyme has specificity constant values of 1.0 × 103, 1.1 × 104, and 4.0 × 10–1 for compounds A, B, and
C, respectively. For which compound does the enzyme have a higher efficiency and why?

a. Compound C; a low kcat value accounts for the high and specific rate of catalysis, while a high KM
value lowers the required concentration of the compound.

b. Compound B; a high KM value accounts for the high and specific rate of catalysis, while a low kcat
value lowers the required concentration of the compound.

c. Compound A; higher kcat accounts for the high and specific rate of catalysis, while a low KM value
lowers the required concentration of the compound.

d. Compound C; the least amount of the compound is required to saturate the enzyme, while having the
highest rate of catalysis.

e. Compound B; the least amount of the compound is required to saturate the enzyme, while having the
highest rate of catalysis.

Answer 16

e. Compound B; the least amount of the compound is required to saturate the enzyme, while having the
highest rate of catalysis.

Question 17

Which constant represents the nature of the enzyme–substrate interaction?
a. specificity constant
b. constant of the catalysis rate
c. Michaelis constant
d. rate constant k1
e. allosteric constant

Answer 17

c. Michaelis constant

Question 18

The specificity constant does NOT depend on the rate constant for the:
a. formation of the ES complex (kcat).
b. dissociation of the ES complex (k–1).
c. formation of the product (k2).
d. formation of the ES complex (k1).
e. formation of the product (kcat).

Answer 18

a. formation of the ES complex (kcat).

Question 19

KM of the cytosolic isomer of fumarase is equal to 5 μM, whereas KM of the mitochondrial isomer is equal
to 50 μM. What should the value of k2 be for a less active isomer of the enzyme to achieve kinetic perfection?
a. from 5 × 108 to 5 × 109
b. from 2 × 107 to 2 × 108
c. from 1 × 108 to 1 × 109
d. from 5 × 102 to 5 × 103
e. from 2 × 106 to 2 × 107

Answer 19

d. from 5 × 102 to 5 × 103

Question 20

What is the ternary complex for the enzyme (E) that converts pyruvate to lactate using NADH as a
cosubstrate?
a. E (lactate) (NAD+)
b. E (NADH) (pyruvate)
c. E (pyruvate) (lactate)
d. E (NADH) (NAD+)
e. E (lactate) (NADH)

Answer 20

e. E (lactate) (NADH)

Question 21

hat is the reaction class if all substrates must bind to the enzyme in an arranged manner before any
product is released?
a. random sequential
b. ping-pong
c. ordered sequential
d. second order

Answer 21

c. ordered sequential

Question 22

An example of a reaction of the double-displacement class is the:

a. conversion of pyruvate and NADH to lactate and NAD+ by lactate dehydrogenase with formation of
a ternary complex.

b. conversion of creatine and ATP to phosphocreatine and ADP by creatine kinase with ATP being
released before both substrates bind the enzyme.

c. conversion of aspartate and α-ketoglutarate to oxaloacetate and glutamate with formation of a ternary
complex.

d. cleavage of a peptide bond by chymotrypsin with the formation of a substituted intermediate on a
serine residue.

e. isomerization of dihydroxyacetone phosphate to glyceraldehyde 3-phosphate.

Answer 22

d. cleavage of a peptide bond by chymotrypsin with the formation of a substituted intermediate on a
serine residue.

Question 23

What is NOT a feature of allosteric enzymes?

a. Their activity can be modified by environmental signals.
b. They have a sigmoidal dependence of the reaction velocity on the substrate concentration.
c. Each allosteric enzyme is capable of conducting multiple reactions.
d. Their activity isn’t regulated by a threshold effect.
e. They depend on alterations in the quaternary structure.

Answer 23

d. Their activity isn’t regulated by a threshold effect.

Question 24

Judging by the given scheme of two metabolic pathways where en denotes different enzymes, give the name
of interactions that regulate the function of these pathways in a coherent fashion.

a. K inhibits e1 and e10 while F inhibits e1, and I inhibits e10.

b. F and I inhibit e1 and e10, respectively, and stimulate e10 and e1, respectively, whereas K inhibits e1and e10.

c. F stimulates e10 and I stimulates e1 while K inhibits e1 and e10.

d. K stimulates e1 and e10 while F inhibits e1, and I inhibits e10.

e. F and I stimulate e1 and e10, respectively, and inhibit e10 and e1, respectively, whereas K inhibits e1
and e10.

Answer 24

b. F and I inhibit e1 and e10, respectively, and stimulate e10 and e1, respectively, whereas K inhibits e1and e10.

Question 25

It is NOT characteristic for the concerted model for allosteric enzymes to: a. catalyze multiple reactions within one enzyme. b. maintain two distinct conformations of the enzyme that can be spontaneously interconverted. c. bind the substrate to the more stable conformation more readily. d. follow the symmetry rule by all of the enzyme active sites. e. disrupt the equilibrium between the conformations in favor of the least stable form after the substrate binding.

Answer 25

c. bind the substrate to the more stable conformation more readily.

Question 26

What is TRUE regarding the action of allosteric effectors? a. Negative effectors inhibit the less stable form of the enzyme. b. Positive effectors stimulate the more stable form of the enzyme. c. Negative effectors stabilize the less stable form of the enzyme. d. Negative effectors inhibit the more stable form of the enzyme. e. Negative effectors stabilize the more stable form of the enzyme.

Answer 26

e. Negative effectors stabilize the more stable form of the enzyme.

Question 27

What is TRUE for the sequential model for allosteric enzymes? a. The binding of a substrate disrupts the equilibrium between two states of the enzyme. b. The initial molecule of the substrate prevents unproductive colliding between other substrate molecules and the tense form of the enzyme. c. The rate constant for the binding of a substrate is lower for the last subunit of the enzyme than for the first one. d. The affinity to the substrate increases due to the influence of neighboring subunits. e. Cooperativity in the sequential model can only be positive.

Answer 27

d. The affinity to the substrate increases due to the influence of neighboring subunits.

Question 28

Which enzyme of the given metabolic pathway is most likely to be an allosteric enzyme that controls the synthesis of metabolite H? a. e1 b. e2 c. e3 d. e5 e. e7

Answer 28

e. e7

Question 29

Which enzyme of the given metabolic pathway is most likely to catalyze a committed step for the synthesis of metabolite D? a. e1 b. e2 c. e3 d. e4 e. e6

Answer 29

c. e3

Question 30

What is the name for allosteric regulation when a molecule blocks the committed step of its own synthesis pathway? a. committed inhibition b. feedback inhibition c. concerted model d. sequential model e. cooperativity

Answer 30

b. feedback inhibition

Question 31

Which type of experiment allows simultaneous studying of millions of enzyme molecules? a. ensemble studies b. cooperative studies c. in singulo d. homotropic e. heterotropic

Answer 31

a. ensemble studies

Question 32

Which type of method allows investigation of molecular heterogeneity? a. homotropic b. ensemble studies c. heterotropic d. in singulo e. cooperative studies

Answer 32

d. in singulo

Question 33

What is the premise of the Michaelis–Menten equation that is achieved by assuming equal rates of formation and breakdown of the ES complex? a. no-reverse-reaction assumption b. investigating the reaction at time close to zero c. steady-state assumption d. assumption of emanations e. equilibrium assumption

Answer 33

c. steady-state assumption

Question 34

An enzyme will be MOST sensitive to changes in the substrate concentration when: a. [S] is near KM. b. [S] is below KM. c. KM is below Vmax. d. [S] is above KM. e. KM is Vmax/2.

Answer 34

b. [S] is below KM.

Question 35

Judging by the given Lineweaver–Burk plot, identify the turnover number of enzyme B if its total concentration is 0.2 M. a. 0.1 b. 10 c. 5 d. –1 e. 2.5

Answer 35

b. 10

Question 35

Judging by the given Lineweaver–Burk plot, identify the concentration of substrate that is required for enzyme A to operate at half of its maximal speed. a. 0.5 b. –0.5 c. -2 d. 2.5 e. 0.4

Answer 35

a. 0.5

Question 36

What is the critical feature of the Michaelis–Menten model of enzyme catalysis? a. increasing the probability of product formation b. shifting the reaction equilibrium c. formation of an ES complex d. reaching the reaction equilibrium e. accumulation of the product

Answer 36

c. formation of an ES complex

Question 37

Which description of the concerted model for allosteric enzymes is TRUE? a. At a low substrate concentration, L0 is small. Upon increasing the substrate concentration, in accordance with the symmetry rule, L0 will be increasing. The disrupted equilibrium of the enzyme states results in a sharp increase of the reaction velocity. As the concentration reaches the threshold, the enzyme becomes more active. b. Upon increasing the substrate concentration, due to cooperativity, the number of enzyme molecules in the T state will be decreasing. The equilibrium between enzyme states is disturbed due to a lower stability of the R state. As the concentration reaches the threshold, the enzyme becomes more active. c. At a low substrate concentration, L0 is large. Increasing the substrate concentration will result in accumulation of the enzyme in the R state, which will increase L0. The disrupted equilibrium of the enzyme states results in a sharp increase of the reaction velocity. When the substrate concentration is way above KM, the enzyme activity is very sensitive to the changes in the concentration, which results in a sharp increase of the reaction velocity. d. Upon increasing the substrate concentration due to the symmetry rule, the number of enzyme molecules in the T state will be increasing. The equilibrium between enzyme states is disturbed due to a lower stability of the T state. When the substrate concentration is way above KM, the enzyme activity is very sensitive to the changes in the concentration, which results in a sharp increase of the reaction velocity. e. At a low substrate concentration, L0 is large. Upon increasing the substrate concentration, L0 will be markedly decreasing. The disrupted equilibrium of the enzyme states results in a sharp increase of the reaction velocity. As the concentration reaches the threshold, the enzyme becomes more active.

Answer 37

e. At a low substrate concentration, L0 is large. Upon increasing the substrate concentration, L0 will be markedly decreasing. The disrupted equilibrium of the enzyme states results in a sharp increase of the reaction velocity. As the concentration reaches the threshold, the enzyme becomes more active.

Question 38

What is the value of [S] as a fraction of KM required to obtain 20% Vmax? a. 0.2 KM b. 0.25 KM c. 0.5 KM d. 0.75 KM e. 0.8 KM

Answer 38

b. 0.25 KM

Question 38

Allosteric effectors alter the equilibrium between the: a. ES state. b. R and T forms of a protein. c. forward and reverse reaction rate. d. formation of the product and its reverse reaction. e. concentration thresholds.

Answer 38

b. R and T forms of a protein.

Question 39

loss of allosteric regulation in the production of purine nucleotides may result in: a. excess nucleotides for DNA. b. a loss of PRS catalytic activity. c. decreased urate degradation. d. a decrease in urate concentration. e. an excess accumulation of urates.

Answer 39

e. an excess accumulation of urates.

Question 40

The formula V0 = Vmax ([S]/[S] + KM) indicates the relationship between the: a. enzyme activity and the equilibrium constant. b. rate of a catalyzed reaction and the equilibrium constant. c. enzyme activity and substrate concentration. d. probable substrate concentration and the normal concentration in vivo. e. turnover number and the rate of catalysis.

Answer 40

c. enzyme activity and substrate concentration.

Question 41

When the substrate concentration is much greater than KM, the rate of catalysis is almost equal to: a. [S] + KM. b. kcat. c. Vmax. d. Vmax/2. e. (Vmax/KM)[S].

Answer 41

c. Vmax.

Question 42

If the enzyme concentration is 5 nM, the substrate concentration is 5 mM, and KM is 5 μM: a. the enzyme will be saturated with the substrate. b. most of the enzyme won't have the substrate bound. c. there will be more enzyme than substrate. d. the enzyme will be displaying first-order kinetics. e. the rate of the reaction will be half its maximal value.

Answer 42

a. the enzyme will be saturated with the substrate.

Question 43

Homotropic effects of allosteric enzymes: a. are due to the effects of substrates. b. are due to the effects of allosteric activators. c. shift the kinetics curve to the left. d. shift the kinetics curve to the right. e. account for the linear nature of the kinetics curve.

Answer 43

a. are due to the effects of substrates.

Question 44

When [S] << KM, the enzymatic velocity depends on: a. the values of kcat/KM, [S], and [E]T. b. Vmax of the reaction. c. the affinity of the substrate for the catalytic site. d. the values of kcat, [S], and [E]T. e. the formation of the ES complex.

Answer 44

a. the values of kcat/KM, [S], and [E]T.

Question 45

.Allosteric effectors: a. can cause large changes in enzymatic activity. b. can lead to a decrease in the availability of a protein. c. don't alter the sensitivity of a metabolic pathway. d. decrease the sensitivity of the enzyme at nearly all concentrations of the substrate. e. alter enzyme activity by binding to the active site of an enzyme.

Answer 45

a. can cause large changes in enzymatic activity.

Question 46

What condition is met when the amount of substrate is far greater than the amount of enzyme present? a. [S] is much less than KM. b. V0 is half of Vmax. c. The enzyme is displaying second-order kinetics. d. The enzyme is displaying first-order kinetics. e. The enzyme is displaying zero-order kinetics.

Answer 46

e. The enzyme is displaying zero-order kinetics.

Question 47

During the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. a. This is an enzyme that displays Michaelis–Menten kinetics and you purify away a homotropic inhibitor. b. This is an enzyme that displays Michaelis–Menten kinetics, and you must use a Lineweaver–Burk plot to determine KM and Vmax correctly. c. This is an allosteric enzyme and you must use a Lineweaver–Burk plot to determine KM and Vmax correctly. d. This is an allosteric enzyme and during purification you purify away a heterotropic activator. e. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates.

Answer 47

d. This is an allosteric enzyme and during purification you purify away a heterotropic activator.

Question 48

Calculate the turnover number for the enzyme if its Mr is 75,000 and if by assaying 5 μg of the enzyme under saturating [S] concentrations, you determine that Vmax is approached asymptotically and is equal to 1.68 μmol/sec. a. 2.25 × 106 sec–1 b. 1.50 × 105 sec–1 c. 2.50 × 105 sec–1 d. 2.52 × 104 sec–1 e. You also need to know KM for this enzyme to calculate the turnover number.

Answer 48

d. 2.52 × 104 sec–1

Question 49

Enzymes

Answer 49

protein catalysts that can accelerate the rate of a reaction by factors of as much as a million or more.

Question 50

Substrates

Answer 50

What reactants in an enzyme are called

Question 51

Hydrolysis

Answer 51

the breaking of a chemical bond by the addition of a water molecule

Question 52

proteolytic enzymes

Answer 52

enzymes that break down protein

Question 53

Trypsin

Answer 53

a proteolytic enzyme that cleaves on the carboxyl side of Arg and Lys residues

Question 54

Thrombin

Answer 54

a proteolytic enzyme that cleaves on Arg-Gly bonds in particular sequences only

Question 55

oxidoreductases

Answer 55

Major class of enzymes that catalyze oxidation-reduction reactions

Question 56

Transferases

Answer 56

major class of enzymes that move functional groups between molecules

Question 57

Hydrolases

Answer 57

major class of enzymes that cleave bonds with the addition of water

Question 58

lyases

Answer 58

major class of enzymes that remove atoms to form double bonds or add atoms to double bonds

Question 59

isomerases

Answer 59

major class of enzymes that move functional groups within a molecuel

Question 60

ligases

Answer 60

major class of enzymes that join two molecules at the expense of ATP

Question 61

Prosthetic groups

Answer 61

tightly bound coenzymes such as the heme group in Cytochrome C

Question 62

holoenzyme

Answer 62

an enzyme with its cofactor

Question 63

cofactor

Answer 63

small molecules that some enzymes require for activity

Question 64

two main classes of cofactors

Answer 64

coenzymes (organic molecules derived from vitamins) and metals

Question 65

apoenzyme

Answer 65

an enzyme that doesn't have its cofactor

Question 66

G (free Energy)

Answer 66

a measure of energy capable of doing work

Question 67

Delta G

Answer 67

Change in free energy; a reaction can be characterized by this energy difference. Will remain the same with or without an enzyme

Question 68

-delta G

Answer 68

a reaction that will occur spontaneously

Question 69

+ delta G

Answer 69

a reaction that will not occur spontaneously and requires something in addition such as ATp

Question 70

Exergonic Reactions

Answer 70

a reaction that will occur without the input of energy, spontaneously. Only if the delta G is negative

Question 71

Endergonic reactions

Answer 71

delta G is positive and the reaction will not occur without the addition of energy

Question 72

Reaction at Equilibrium

Answer 72

no net change in the amount of reactant or product. Delta g = 0

Question 73

More -delta G

Answer 73

The larger the equilibrium constant will be, The more exergonic the reaction

Question 74

Transition State

Answer 74

a molecular form that is no longer substrate but not yet product. designated by the double dagger

Question 75

Activation energy

Answer 75

The energy required to form the transition state from the substrate. symbolized by delta g double dagger

Question 76

How do enzymes help

Answer 76

Facilitating the formation the transition state and decreasing the activation energy

Question 77

Substrate Changes

Answer 77

substrate changes structure so it can get to transition, if there is enough energy to get over the hill then it will have enough energy to form the product but it cant go in reverse

Question 78

ES-complex

Answer 78

enzyme-substrate complex: enzymes bring substrates together to form this on a particular region

Question 79

Active site

Answer 79

The particular region of the enzyme that is formed with the ES-complex

Question 80

Enzyme and substrate(s)

Answer 80

The interaction of these two molecules at the active site promotes the formation of the transition state

Question 81

Common Features of Enzyme Active Sites

Answer 81

1. Active site is a 3-D cleft or crevice created by amino acids from different parts of the primary structure 2. The active site constitutes a small portion of the enzyme volume 3. Active sites create unique microenvironments 4. The interaction of the enzyme and substrate at the active site involves multiple weak interactions 5. Enzyme specificity depends on the molecular architecture at the active site

Question 82

Induced fit

Answer 82

Enzyme changes shape upon substrate binding

Question 83

The velocity of a reaction is the quantity of the: a. reactant that appears in a specified unit of time. b. product that disappears in a specified unit of time. c. solution color that disappears in a specified unit of time. d. reactant that disappears in a specified unit of time. e. solution color that appears in a specified unit of time.

Answer 83

d. reactant that disappears in a specified unit of time.

Question 84

What is the reaction order if the reaction rate was doubled by doubling the reactant concentration? a. zero order b. first order c. second order d. pseudo-first order e. pseudo-second order

Answer 84

b. first order

Question 85

What is the reaction order if the reaction rate was increased by a factor of 4 by doubling the reactant concentration? a. zero order b. first order c. second order d. pseudo-first order e. pseudo-second order

Answer 85

c. second order

Question 86

Which rate equation is TRUE if doubling the concentration of reactant A doubles the reaction rate and doubling the concentration of reactant B has no effect on the rate? a. V = k[A] b. V = k[A][B] c. V = k[A]2[B]1 d. V = k[A]2[B] e. V = k[A]2

Answer 86

a. V = k[A]