Exam 3 – Fall 2019
BCH 341 - Physical Chemistry with a Biological Focus
Professor Jeff Yarger
September 4-7, 2019
DUE Monday October 7, 2019 by 11:59 PM (UTC-7). Turn in completed exam as a typeset single PDF
document into the assignment link on ASU Canvas. Please make sure the completed exam is organized,
self-contained and all text, equations, numbers, units, figures and images are typeset, clear and legible.
Student Required Identification:
NAME:___rubric/key________________________________________ ASU ID #:________________________________________________ (10-digit number (typically starting with 12xxxxxxxx or 10xxxxxxxx)) Email: [email protected]_________________________
Exam General Instructions There are 4 multi-component exercises/projects on this exam. Each of the multi-component numbered
exercises/projects (problems) is worth 25 points. Hence, the exam is worth a total of 100 points. You are required
to explicitly show all equations, numerical calculations and associated units. All points are associated with
explicitly showing all your work and no points are awarded for just determining the correct numerical answer.
All assumptions need to be clearly and concisely stated. If thermodynamic parameters are used, the citation,
reference or link to where this thermodynamics data came from must be stated. Appropriate units should be
associated with all numerical problem solving. The completed exam should be typeset (no handwriting of
equations or numerical values and associated units).
Evaluation Section (TA/Instructors) Instructor Comment:
___________________________________________________________________________________________
___________________________________________________________________________________________
___________________________________________________________________________________________
___________________________________________________________________________________________
Instructor Grading Summary:
Exam Score: ________ / 100 pts Extra Credit: ________ / 15 pts
Page 2
1. Malate dehydrogenase (MDH) is an enzyme that reversibly catalyzes the oxidation of malate to oxaloacetate
using the reduction of NAD+ to NADH. This reaction is part of many metabolic pathways, including the citric
acid cycle. (A) Write a balanced chemical reaction and the associated half-reactions for the oxidation of malate to
oxaloacetate using the reduction of NAD+ to NADH. (10 pts) (B) Calculate the biological standard Gibbs energy
for the balance chemical reaction of the oxidation of malate to oxaloacetate using the reduction of NAD+ to
NADH. (15 pts)
This exam question was directly adopted from the Fall 2019 BCH341 suggested homework problem 5.35(b) -
Atkins and De Paula, Physical Chemistry for the Life Sciences, 2nd Ed. p. 214.
Also, there is a YouTube video created as part of an Honors Contract that covers 5.35(b) and is posted (with the
student's permission) on the biopchem channel:
https://youtu.be/cfnInDizyvY
The solution given by Trapp and Cady, Solution Manual to Accompany Physical Chemistry for the Life Sciences,
2nd Ed., for 5.35(b) is provided below:
Other than showing explicitly showing both 1/2 reactions, this basically covers the solution for problem 1.
There are a lot of sources that can be used to get the biological standard potentials, including Table 5.2 in Atkins
textbook. This is what was used to determine the reaction standard potential used in the solution manual (but not
explicitly calculated). As long as the source for the biological standard potentials used by students is given and
can be verified, it should be allowed. From values I have found in other textbooks and online, the values can vary
by ~10%.
Page 3
2. The standard potentials of proteins can be determined using a solution method by allowing the oxidized protein
to react with an appropriate electron donor and then using the Nernst equation, the equilibrium concentrations of
all species in solution, and the known standard potential of the electron donor. We shall illustrate this method
with the protein cytochrome c.
(A) The one-electron reaction between cytochrome c, cyt-c and 2,6-dichloroindophenol, D, can be written as
cyt-cox + Dred ⇌ cyt-cred + Dox
Consider Eocyt and EoD to be the standard potentials of cytochrome c and D, respectively. Show that, at
equilibrium (eq), a plot of ln([Dox]eq/[Dred]eq) against ln([cyt-cox]eq/[cyt-cred]eq) is linear with a slope of 1 and y-
intercept F(Eocyt-EoD)/RT, where equilibrium activities are replaced by the numerical values of equilibrium molar
concentrations. (10 pts)
(B) The following data were obtained for the reaction between oxidized cytochrome c and reduced D at pH 6.7
buffer and 298 K. The ratios [Dox]eq/[Dred]eq and [cyt-cox]eq/[cyt-cred]eq were adjusted by adding known volumes of
a solution of sodium ascorbate, a reducing agent, to a solution containing oxidized cytochrome c and reduced D. From the data and the standard potential of D of +0.237 V, determine the standard potential of cytochrome c at
pH=6.7 and 298 K. Show and describe all plots and fits of the data for full credit. (15 pts)
[Dox]eq/ 0.0031 0.0085 0.0257 0.0497 0.0953 0.2380 0.5330 [Dred]eq
[cyt-cox]eq/ 0.0110 0.0310 0.0894 0.1970 0.3350 0.8090 1.8850 [cyt-cred]eq
This exam question was adopted from the Fall 2019 BCH341 suggested homework problem (project) 5.52 -
Atkins and De Paula, Physical Chemistry for the Life Sciences, 2nd Ed. p. 215. The data values and pH are
different than what is given in Atkins project 5.52. However, if a student had completed the suggested homework
before taking exam 3, and used a spreadsheet or scientific plotting package to complete 5.52, then this should be a
great starting point and an easy modification to redoing the plot, linear fit and associated calculations using the
new values given in part (B) of this exam problem.
Therefore, a plot of ln([Dox]eq/[Dred]eq) against ln([cyt-cox]eq/[cyt-cred]eq) is linear with a slope of 1 and y-
intercept F(Eocyt-EoD)/RT.
Page 4
A public shared Google Sheet is available from BioPchem ([email protected]):
https://docs.google.com/spreadsheets/d/17emwcxGd11Bqr3YiEUwDogqTPnurchJWKxFXu1ww_ps/edit
?usp=sharing
A reduced screenshot of the bottom part of this Google Sheet is shown below:
Eocyt = 204.4 mV
Page 5
3. (A) Make an appropriate Arrhenius plot of the following data for the binding of an inhibitor to the enzyme
carbonic anhydrase and calculate (B) the activation energy and (C) the pre-exponential factor for the reaction.
Show and describe all plots and fits of the data for full credit. (A) 10 pts, (B) 10 pts and (C) 5 pts.
T/K 275 285 295 305 315 325 kr/(106 dm3 mol-1 s-1) 1.01 1.22 1.55 1.91 2.35 2.85
This exam question was adopted from the Fall 2019 BCH341 suggested homework problem 6.39 - Atkins and De
Paula, Physical Chemistry for the Life Sciences, 2nd Ed. p. 241.
The solution given by Trapp and Cady, Solution Manual to Accompany Physical Chemistry for the Life Sciences,
2nd Ed., for 6.39 is provided below:
The temperature and reaction rate data are different, but this is a simple change to make if students have
completed 6.39 using a standard spreadsheet app or scientific plotting app. A publicly shared Google
Sheet is provided to illustrate this:
https://docs.google.com/spreadsheets/d/1D29MG6GOU3AOJkRV_1k-
D_VrKk8kgqBsp7j6_gUXTpE/edit?usp=sharing
Page 7
4. Prebiotic reactions are reactions that might have occurred under the conditions prevalent on the Earth before the
first living creatures emerged and can lead to analogs of molecules necessary for life as we now know it. To
qualify, a reaction must proceed with a favorable rate and have a reasonable value for the equilibrium constant.
An example of a prebiotic reaction is the formation of 5-hydroxymethuracil (HMU) from uracil and
formaldehyde. Amino acid analogs can be formed from HMU under prebiotic conditions by reaction with various
nucleophiles, such as H2S, HCN, indole and imidazole. For the synthesis of HMU at pH = 7, the temperature
dependence of the rate constant is given by
log kr/(106 dm3 mol-1 s-1) = 11.8 - 5500/(T/K)
and the temperature dependence of the equilibrium constant is given by
log K = -1.4 + 1800/(T/K)
(A) Calculate the rate constants and equilibrium constants over a range of temperature corresponding to possible
prebiotic conditions, such as 0-50oC, and plot them against temperature. (10 pts) (B) Calculate the activation
energy and the standard reaction Gibbs energy and enthalpy at 25oC. (10 pts) (C) Prebiotic conditions are not
likely to be standard conditions. Speculate about how the actual values of the reaction Gibbs energy and enthalpy
might differ from standard values. Do you expect that the reaction would still be favorable? (5 pts)
This exam question was adopted from the Fall 2019 BCH341 suggested homework problem (project) 6.42 -
Atkins and De Paula, Physical Chemistry for the Life Sciences, 2nd Ed. p. 242.
The solution given by Trapp and Cady, Solution Manual to Accompany Physical Chemistry for the Life Sciences,
2nd Ed., for 6.42 is provided below:
Page 10
A publicly shared Google Sheet is provided: https://docs.google.com/spreadsheets/d/1Vxqai4RP2sD9XpJ4p7_BG7CpCyxX_67XJHMrN-
zOhWA/edit?usp=sharing
A screenshot is shown below:
Page 11
Extra Credit: (15 pts) There are numerous scientific journal articles that cover all the topics and problems on this
exam. Going back and looking at the original experiments, data, data analysis, plots, calculations, etc can be an
excellent source to better and more fully understand a specific topic. For example, problem 3 on this exam is
basically the same as suggested homework problem 6.39, except the data provided is different. This difference in
data is because there are several isoenzymes of carbonic anhydrase. This comes from a specific journal article
and the citation is given below. Look up this journal article and read it over. Compare the data given in
homework problem 6.39 and in problem 3 on this exam, with the data provided in the journal article for human
isoenzymes B and C. Can you predict whether the data given in homework problem 6.39 was uncatalyzed or a
catalyzed reaction? and what about the data from problem 3 on this exam?
G. Sanyal, T. H. Maren, Thermodynamics of Carbonic Anhydrase Catalysis: A Comparison Between Human
Isoenzymes B and C. The Journal of Biological Chemistry, 256(2), 608-612 (1981).