Exercises (from Atkins, Physical Chemistry, 8th Edition) and equations

Half-life for a second-order reaction Arrhenius equation Collision theory

k = A exp Ea RT t1/2 = 1/(k[A]0 )

Reaction Gibbs energy

G = H T S

(Chapter 24, exercises 1 a/b, 2 a/b, 3 a/b, 4 a/b, problems 1,2,3)

Collision frequency: z = rel NA c Cross-section: = d2 Reactive cross-section: = P Relative mean speed:

crel = 8kB T = 8RT NAv

Collision density for reaction A+A: ZAA = 0, 5zNA Collision density for reaction A+B: ZAB = zNB Fraction of collisions, occuring with energy exceeding :
N /N = P () = exp[ /(kB T )] = exp[E /(RT )]

Bimolecular rate constant: Transition state theory

exercises 15 a/b)

k = crel NAv eEa /(RT )

(Chapter 24, exercises 10 a/b, 11 a/b, 12 a/b, 14 a/b, Chapter 22,

Bimolecular rate constant:

k= kB T RT exp h p0 G RT = kB T RT exp h p0 S R exp H RT

Arrhenius parameters for gases:

Ea = H + 2RT and A = kB T RT 2 e exp h p0 S R

Arrhenius parameters for liquids:

Ea = H + RT and A = kB T RT e exp h p0 S R h 4 kf

Zero-point energy (for estimating the kinetic isotope eect): Kinetic derivations

E0 =

(Chapter 23, exercises 1 a/b, 2 a/b, 4 a/b, 5 a/b, theoretical problems 2 and numerical problems 3)

Enzyme kinetics

(Exercises next page)

Michaelis-Menten-equation: Competitive inhibition:

v=

v=

vmax [S] [S] + KM

or

v=

vmax 1 + KM /[S]

vmax vmax [S] = 1 + (KM /[S]) (1 + [I]/KEI ) [S] + KM (1 + [I]/KEI )

Uncompetitive inhibition:
v= vmax [S]/ (1 + [I]/KESI ) [S] + KM (1 + [I]/KESI )
or

v=

vmax 1 + (KM /[S]) + ([I]/KESI )

Mixed inhibition:
v = vmax [S]/ (1 + [I]/KESI ) = [S] + KM (1 + [I]/KESI ) vmax 1 + (KM /[S]) (1 + [I]/KEI ) + ([I]/KESI )

Photochemistry

(Chapter 23, exercises 7 a/b, 8 a/b, problems 6, 21, 18)

Overall quantum yield:

=
number of products rate of production = number of photons absorbed Iabs

Energy of a photon: E = h = hc/ Absorbance: A = log(I0 /IT ) Surface reactions

(Chapter 25, exercises 813 a/b)

Langmuir adsorption isotherm:

= Kp/(1 + Kp) ln K2 Hadsz,m = K1 R 1 1 T2 T1

Temperature dependence of the equilibrium constant: Kinetic description of desorption: Kinetics of reactions in solution
15 a/b)

t1/2 = 0 eEdesz /(RT )

(Chapter 24, exercises 5 a/b, 6 a/b, 7 a/b, 8 a/b, 9 a/b,

Rate coecient for a diusion-controlled reaction: kd = 4NA RAB DAB Viscosity dependence of rate coecients: kd = 8RT /(3) Stokes-Einstein relation: D = kB T /(6R) Ionic strength dependence of rate coecients: lg k = lg k + 2zA zB A I Dynamic electrochemistry
22 a/b, 26 a/b) (Chapter 25, exercises 16 a/b, 17 a/b, 18 a/b, 19 a/b, 20 a/b,

Limiting current density: |jh | = |zF Dc/| Estimation of D from the ionic conductivity: = z 2 F 2 D/(RT ) Butler-Volmer-equation: j = j0 e(1)zf ezf The low overpotential limit: j j0 zf Tafel plot: ln j = ln j0 + (1 ) z f , and ln j = ln j0 z f
2

Fundamental constants
R h c
8.314 6.626 1034 2.998 108

J mol K Js m/s

kB p0

1.381 1023 101325

J/K Pa

NA F

6.022 1023 96485

mol1
C/mol

Source:

R. Chang, Physical Chemistry for the Biosciences, USB, Sausalito, 2005

Exercises on enzyme kinetics

1. Measurements of a certain enzyme-catalyzed reaction with k1 = 8 106 M1 s1 , k1 = 7 104 s1 , and k2 = 3 103 s1 follows the scheme below:
1 E + S ES

v1 = k1 [E][S] v1 = k1 [ES] v2 = k2 [ES]

ES E + S ES T + E
k2

k1

Does the enzyme-substrate binding follow the equilibrium or steady-state scheme? 2. Derive the following equation from the Michaelis-Menten equation:

v vmax v = [S] KM KM
and show how you would obtain the values of KM and vmax graphically from this equation. 3. An enzyme with KM = 3.9 105 M is studied at an initial substrate concentration of 0.035 M. After 1 min, it is found that 6.2 M of product has been produced. Calculate the value of vmax and the amount of product formed after 4.5 min. 4. Penicillinase catalyzes the decomposition of some antibiotics. How many active sites does the enzyme have if 6.4 g penicillinase catalyzes the destruction of 3.11 mg antibiotic (Mr = 364) in 20 s at 28 C? The molar mass of penicillinase is 30 kg/mol, k2 = 2000 s1 . 5. The acetylcholinesterase is an enzyme with a single active site that metabolizes acethylcholine. How many grams of acetylcholine can 2.16 g acetylcholinesterase in one hour? (k2 = 14000 s1 , Mr (enzyme) = 42 kg/mol and the molecular formula of acetylcholine is C7 NO2 H+ .) 16 6. An enzyme has KM = 2.8 105 M and vmax = 53 M/min. Calculate v0 if [S]0 = 3.7 104 M and [I]0 = 4.8 104 M for (a) a competitive inhibitor, (b) an uncompetitive inhibitor and (c) noncompetitive inhibitor with K = 1.7 105 M for all cases. 7. The metabolism of ethanol in our bodies is catalyzed by enzyme LADH to acetaldehyde and nally to acetate. In contrast, methanol is converted to formaldehyde which can cause blindness or even death. An antidote for methanol is ethanol which acts as a competitive inhibitor. How much absolute ethanol has to be consumed by the person after ingesting 50 mL of methanol to reduce the activity of LADH to 3 % of the original value? Assume that the total uid volume in the person's body is 38 liters and the density of ethanol and methanol are 0.789 g/mL and 0.791 g/mL, respectively. For methanol KM = 1.0102 M and for ethanol KI = 1.0 103 M. 3