Chapter 4

1. 1. D. The expansion of a gas into vacuum is an entropic phenomenon. There is

effectively no interaction between molecules in the gaseous state, regardless of
concentration. Hence, no enthalpy change. Also, H = U + pV. If q = 0, H =
pV + pV = 0. When two objects come to equilibrium, say two pieces of
metal, heat is exchanged between them but there is no change in the structure of
the metals unless, of course, the coming to equilibrium results in a phase
change Also, the heat is exchanged between the objects, not the surroundings,
so q = 0 for the combined system and H = 0.
2. C. There is an increase in entropy when two objects coming to equilibrium
because heat is transferred from an object at one temperature to an object at
another temperature.
3. C. Work would have to be done to compress the expanded gas, and work
would have to be done to restore the objects to their original temperatures. Thus,
both processes involve a decrease in free energy.
4. D. Both changes are spontaneous in one direction only.
2. 1. A. When temperature and pressure are constant, and G is negative, the
process is spontaneous. A negative free energy says nothing about reversibility.
2. D. S < 0 says nothing about the reversibility of the process. The total
entropy (system plus surroundings) must increase for spontaneity, not decrease.
3. B. The work a system can do is maximal when a process it undergoes is
reversible, i.e., at equilibrium. Under such conditions, the entropy change is
minimal.
4. A. Dilution is spontaneous. As with the expanding gas in the previous
problem, work would have to be done to concentration the solute after dilution.
5. B. S = q / T, but only if the process is reversible. When a process is
reversible, measurement of T and q enables indirect determination of S.
6. B. Inefficient coupling results in things like the generation of heat due to
friction and the like; in a word, irreversibility. For a reversible process, i.e., a
process at equilibrium, G = Ginput + Goutput = 0. So Goutput = Ginput. The
efficiency of a process scales as 100%(Goutput/Ginput). For a spontaneous
process, G = Ginput + Goutput < 0, so Goutput < Ginput, and the efficiency is
less than 100%.
3. 1. C. Both U and G are state functions, as are U and G.
2. A. q + w = U. This is a mathematical statement of the First Law.
3. B. When T and p are constant, G is the appropriate thermodynamic potential
function. A potential function indicates the direction of spontaneous change.
4. D. The disorder function is S.
5. B. When a system is at equilibrium and T and p are constant, there is no
tendency to change. The potential function, G, must be zero.
6. B. One sums the Gs of the component reactions. If the overall change in free
energy is negative, the process will be spontaneous.
7. B. G measures the maximum amount of work that the system can do at
constant T and p.
4. 1. B. This comes from G = 0 at equilibrium.

2001-2007 by D.T. Haynie. All rights reserved.

2. B. This is based on , which itself comes from G.

3. D. For a spontaneous change, G < 0. G is equal to zero only if T = 0 or
Keq = 1.
4. A. H and S are not standard state functions.
5. C. Both G and G are measured in units of energy mol1.
6. A. There is no requirement that products or reactants be in the standard state.
7. B. There are two components to G: a concentration independent one (G)
and one that depends on concentration. The magnitudes of the components are
equal and opposite at equilibrium.
5. 1. A. The activity, or effective concentration, is defined as the product of the
concentration and the activity coefficient.
2. A. G = G + RTln(aproducts/areactants).
3. B. n gives the contribution of n moles of a component of solution to the
overall free energy.
6. The Sun is not absolutely necessary for life on Earth or anywhere. In general
terms, all that is needed for an organism to thrive is a suitable supply of negative
entropy (high free energy chemical compounds, food). Suppose the thermal
energy of Earth were to be tapped as a major source of energy. In principle this is
certainly possible. An effect, however, would be to decrease the temperature of
the surface, requiring us to find more energy to keep warm!
7. The units depend on the chemical reaction. When the number of reactants is the
same as the number of products, Keq is unitless.
8. Go = RTlnKeq
For instance, Go = 8.314 J K1 mol1 298 K ln(0.001) = 17.1 kJ mol1
Keq
0.01
0.1
1
10
100
1000

Go
11.4
5.7
0
5.7
11.4
17.1

9. So = (Go Ho) / T
= (3.3 kcal mol1 + 6 kcal mol1) / 298 K = 31 cal mol1 K1
10. Keq = exp(Go / RT)
= exp((Ho TSo) / RT)
= exp((150 cal mol1 298 K 4.4 cal mol1K1) / (1.9872 cal mol1K1 298 K))
= 7.1
11. B. Cellular conditions will ordinarily differ substantially from those of the
standard state, and this must be taken into account when computing G. Usually,
S data are not available. The only sensible choices are therefore B and E. The
latter, however, does not take the logarithm of K.

2001-2007 by D.T. Haynie. All rights reserved.

12. Suppose you have the reaction A + B C + D, and let Keq << 1. The reaction
proceeds to the left unless there is another route by which the concentration of C
or D can be altered. For depletion of either C or D will result in the conversion of
A and B to C and D, even if this requires getting over a large free energy barrier.
Biochemical reactions are so complex because the product of one reaction is the
reactant of another, possibly several others.
13. We require that the reaction occur in dilute aqueous solution and yield n H2O
molecules:
A + B C + D + nH2O
Because the solution is dilute, [H2O] = 55.5 M. Now, by Eqn. 4.39 and the
reasoning leading to it,
G' = G + nRTln[H2O]
= G + 1 mol 8.314 J K1 mol1 298.16 K ln(55.5 M)
= G + 9.96 kJ mol1
14. G' is larger than G by about 10 kJ mol1 when one mole of water molecules
is produced by the reaction. This must be taken into account because our known
quantities are primes and the unknowns are not. Using Eqn. 4.39,
G' = G + nRTln[H2O]
G = RTlnKeq = G' nRTln[H2O]
In hydrolysis water molecules are consumed, so n, the number of water molecules
produced, is negative.
The hydrolysis of phosphoenolpyruvate yields pyruvate and phosphate, and one
molecule of water is consumed. Using the result of the previous problem and
plugging in known values gives:
Keq = exp((61.9 kJ mol1 (1) 9.96 kJ mol1) / (0.008314 kJ mol1 298
K) = 12.7108
The calculation is similar for pyrophosphate:
Keq = exp((33.5 kJ mol1 + 9.96 kJ mol1) / (0.008314 kJ mol1 298 K)
= 13.4103
And for glucose-1-phosphate:
Keq = exp((20.9 kJ mol1 + 9.96 kJ mol1) / (0.008314 kJ mol1 298 K)
= 82.7
Note that the driving force for hydrolysis of phosphoenolpyruvate is much greater
than that of glucose-1-phosphate. Phosphoenolpyruvate is a product of Reaction 9

2001-2007 by D.T. Haynie. All rights reserved.

of glycolysis, the metabolism of glucose (Chap. 5). Glucose-1-phosphate is a

direct product of glycogen breakdown. Conversion to glucose-6-phosphate
enables the sugar to enter the glycolytic pathway. Pyrophosphate is a product of
DNA synthesis (and other biochemical reactions), as only one phosphate group of
a nucleotide is incorporated into the sugar-phosphate backbone of the nucleic acid.
15. The reaction of interest is FBP GAP + DHAP.
Keq' = [GAP][DHAP]/[FBP]
= [GAP]([DHAP]/[GAP])/([FBP]/[GAP])
= exp(G'/RT)
Solving for [FBP]/[GAP] gives
[FBP]/[GAP] = [GAP] 5.5 / exp(G'/RT)
When [GAP] = 2105 M, we have
[FBP]/[GAP] = (2105 M 5.5) / exp(22.8 kJ mol1/(0.008314 kJ mol1
310 K)) = 2105 M 38,219 M1 = 0.8
and when [GAP] = 1103 M,
[FBP]/[GAP] = 1103 M 38,219 M1 = 40
Note that a two-orders of magnitude increase in the concentration of [GAP] can
give a two-orders of magnitude increase in [FBP]/[GAP], if [DHAP] is
constrained to vary proportionally with [GAP]. What sort of biochemical control
mechanism can impose such a constraint?
16. In Section H we found that G for the reaction given by Eqn. 4.35 at 298 K is
7.3 kJ mol1. By Eqn. 4.32,
G = G + RTln([G6P]/[G1P])
= 7.3 kJ mol1 + (8.314 J mol1 K1 298 K ln(1 mM/0.01 mM)
= 4.1 kJ
The direction of the reaction has been reversed by adjusting the concentrations of
reactants and products. Control of the concentration of a metabolite is an
important means of regulating the flux of matter through biochemical reaction
pathways.
17. From Table 4.6, V' for this reaction is 0.19 V + 0.32 V = +0.13 V, the sum of
the two relevant half-cell reduction potentials. We can calculate the effect of
requiring the concentrations of oxidant and reductant to be certain values using
Eqns 4.75 and 4.76.
[lactate]/[pyruvate] = [NAD+]/[NADH] = 1

2001-2007 by D.T. Haynie. All rights reserved.

This is the trivial case. ln(1) = 0 and V = V for each half reaction; each couple
is 50% reduced. As before, the potentials sum to 0.13 V, and by Eqn. 4.69 the
free energy change is 25.1 kJ mol1.
[lactate]/[pyruvate] = [NAD+]/[NADH] = 160
Vlactate,pyruvate = 0.19 V (RT/2F)ln(160) = 0.19 V ((8.314 J mol1 K1 298
K) / (2 96,494 J V1 mol1)) ln(160) = 0.255 V
VNAD+/NADH = 0.32 V (RT/2F)ln(1/160) = 0.32 V ((8.314 J mol1 K1 298
K) / (2 96,494 J V1 mol1)) ln(1/160) = 0.255 V
By Eqn. 4.77,
V = Vlactate,pyruvate VNAD+/NADH = 0.255 V (0.255 V) = 0.00 V. G must
be zero as well.
[lactate]/[pyruvate] = [NAD+]/[NADH] = 1000
Vlactate,pyruvate = 0.19 V (RT/2F)ln(1000) = 0.19 V ((8.314 J mol1 K1 298
K) / (2 96,494 J V1 mol1)) ln(1000) = 0.279 V
VNAD+/NADH = 0.32 V (RT/2F)ln(1/1000) = 0.32 V ((8.314 J mol1 K1
298 K) / (2 96,494 J V1 mol1)) ln(1/1000) = 0.231 V
V = Vlactate,pyruvate VNAD+/NADH = 0.279 V (0.231 V) = 0.048 V
G = 2 96,494 J V1 mol1 0.048 V = 9.3 kJ mol1
Here, the overall reaction is not spontaneous; the NAD+/NADH half-reaction has
the more positive reducing potential. Lactate is now the reducing agent.
Production of NAD+ requires G < 0 or V > 0. If [NAD+]/[NADH] = 1000, then
VNAD+/NADH = 0.231 V. Setting
Vlactate,pyruvate = 0.19 V (RT/2F)ln(x) = 0.19 V ((8.314 J mol1 K1 298 K)
/ (2 96,494 J V1 mol1)) ln(x) = 0.231 V
and solving for x gives
x = exp((0.231 V + 0.19 V)(2 96,494 J V1 mol1)/(8.314 J mol1 K1 298
K)) = 24
The maximum value of [lactate]/[pyruvate] for production of NAD+ when
[NAD+]/[NADH] = 1000 is 24.
18. From Table E in Appendix C, G' for the conversion of isocitrate into ketoglutarate is 21 kJ mol1. This reaction involves NAD+ and NADH as shown
schematically in Fig. 5.3. G' = G because water is not involved in the

2001-2007 by D.T. Haynie. All rights reserved.

reaction; there is no change in pH if it is assumed that the carbon dioxide

produced by the reaction does form carbonic acid.
From Eqn. 4.32,
G = G + RTln([-KG][NADH]/([NAD+][IC])) = 21 kJ mol1 + 8.314 J mol1
298 K ln((0.1 mM) / 8 / 0.02 mM) = 22 kJ mol1 < 0.
This reaction is a site for metabolic control because G is negative. Moreover
isocitrate dehydrogenase, the enzyme that catalyses this reaction, is strongly
inhibited in vitro by NADH, a product of the reaction. In contrast, most of the
other reactions of the citric acid cycle have G 0.
19. If the two liquids are the same there is no change in concentration on mixing.
There isnt even a change in volume. If follows that there is no change in entropy.
All particles interact with each other as before, so there is no change in enthalpy.
It follows that there is no change in free energy. This is known as the Gibbs
paradox.
20. Let the volume of one bulb be v. The entropy change is given by S = Rln(2v/v) =
Rln2. Assuming the gas to be relatively dilute prior to expansion (or requiring
that the gas be ideal), H = 0. G = H TS = RTln2. As required, the final
state has a lower free energy than the initial one.
21. The sign of the chemical potential of species A and species B in Eqn. 4.31 is
negative. These species are reactants, and we are interested in the difference in
driving force between the products of the reaction and the reactants. In Eqn. 4.32
the negative sign is missing for the reactant terms because lnx1 = lnx, and (
lnx) = +lnx.
22. Cyt f: 3+ 2+ Vo' = 0.365 V, and Cyt c: 3+ 2+ Vo' = 0.254 V.
For the reaction
Cyt c (Fe2+) + Cyt f (Fe3+) Cyt c (Fe3+) + Cyt f (Fe2+)
Vo' = 0.365 V 0.254 V = 0.111 V.
Go' = nFVo' = 1 96,494 kJ V1 mol1 0.111 V = 10711 kJ mol1.
Because Go' < 0, the reaction proceeds spontaneously under standard state
conditions.
23. V = 0.32 V + (8.314 J mol1 K1 310 K) / (2 96249.4 J V1 mol1) ln(1/99)
= 0.38 V
24. Can any other thermodynamic function besides the Gibbs free energy predict the
direction of spontaneous change under the conditions of constant temperature and
pressure? Lets see what the thermodynamics of the liquid to solid transition of

2001-2007 by D.T. Haynie. All rights reserved.

water in the vicinity of the freezing point at one atmosphere pressure can tell us.
U is negative above, at, and below zero, so while the magnitude of U may be
important, sign alone does not predict the direction of spontaneous change. Ditto
for H. Same again for S. The only qualitative difference between these
possibilities and TS is the change in sign. In contrast, G has one sign where we
expect spontaneous change, the opposite sign where we expect the reaction to
move in the opposite direction, and is zero at the melting point. DG would be less
useful to us in predicting the direction of spontaneous change if the constraints
were not temperature and pressure but, say, temperature and volume or volume
and pressure. Biochemists, however, almost always work under the constraints of
constant temperature and pressure.
25. As we have seen, addition of an impurity will in general decrease the melting
point of a pure substance. So, although the presence of cholesterol makes a
membrane more rigid, it also reduces its transition temperature; the overall effect
is relatively little change in melting temperature from pure lipid. Moreover, the
impurity increases the breadth of the phase transition, meaning that it occurs
over a range of temperatures. Nevertheless, a biological will be more rigid at
body temperature with cholesterol present than without it.
26. Bacteria, fish, and other organisms might deal with the effect of changes in the
surrounding temperature by altering the composition of cell membranes in real
time. Steroids like cholesterol are one means of doing this. The rigid compound
affects membrane rigidity and melting temperature.
27. An important design criterion for a liposome-based drug-delivery system is
membrane rigidity. As discussed in the text and in the answer to Exercise 24 of
this chapter, membrane rigidity is influenced by the length of the hydrocarbon tail
and number of unsaturated bonds in a lipid and by the presence of lipo-soluble
materials like steroids. One could adjust the proportions of various possible
components of a membrane to make liposomes with the desired physical
properties.
28. logKeq = 8.188 (2315.5/T) 0.01025T
= 8.188 (2315.5/298) 0.01025 298
= 2.637
G = RTlnKeq
= (1.9872 cal mol1K1) (298 K) 2.303 logKeq = 3.596 kcal mol1
lnKeq (Ho/R)(T2)(T) 2.303logKeq
logKeq + logKeq = 8.188 2315.5 (T + T)1 0.01025 (T + T)
= 8.188 2315.5 (T1 T2T + ) 0.01025 (T + T)
lnKeq / T Ho / RT2 2.303 (2315.5T2T 0.01025T) / T
Ho 2.303 R (2315.5 0.01025T2)

2001-2007 by D.T. Haynie. All rights reserved.

Ho(25 oC)
2.303 1.9872 cal1 mol1 K1 (2315.5 K 0.01025 K1 (298 K)2)
= 6.43 kcal mol1
So(25 oC) = (Go(25 oC) Ho(25 oC)) / T
(3.596 kcal mol1 6.431 kcal mol1) / 298 K = 9.51 cal mol1 K1
Ho + (Ho) = 2.303 R (2315.5 0.01025 (T + T)2)
(Ho) / T 2.303 R 0.01025 2T
Cp(25 oC) (Ho(25 oC)) / T
2.303 1.9872 cal mol1 K1 0.01025 K1 2 (298 K)
= 28.0 cal mol1 K1
29. 1. D. Neither the chemical potential of the solvent nor that of the solute equals
just RTlna.
2. C. Both chemical potentials are equal to o + RTlna.
3. C. At equilibrium, both chemical potentials have the same value on either side
of a membrane.
4. A. The chemical potential of the solute determines the osmotic pressure. This
subject, however, is not dealt with until Chap. 5.
30.
x
0.106
0.107
0.108

ln(1 + x)
0.101
0.102
0.103

% difference
4.95
5.00
5.04

Note: values in the table have been rounded to three

significant figures.

When x is about 0.11, the difference between x and ln(1 + x) is about 5%. This
provides a useful rule of thumb for making the approximation ln(1 + x) x.
31. 1.
2.
3.
4.
5.

C
C
B
D
C

32. KG = [Gln]/([Glu][NH4+]) = 0.00315 (M1)

The M is given in parenthesis to emphasize that the equilibrium constant is
unitless. (For further information on this, see for example Chap. 7 of Atkins,
Physical Chemistry, 6th edn.) The importance of this lies in the choice of
concentration scale. For if the concentrations are in units other than mol/L, for
instance mmol/L, then the argument of the logarithm in the calculation of G will
be different, and G will be different. But G is a state function, so how could its

2001-2007 by D.T. Haynie. All rights reserved.

value depend on the choice of concentration scale? It does not. The difficulty
here is that important information is not shown explicitly. And that is that each of
the concentrations given in the equilibrium constant calculation must be referred
to the standard state concentration, usually 1 M (as discussed in the text).
Kcoupled = [Gln][ADP][Pi]/([ATP][Glu][NH4+]) = KGKATP = 1200
KATP = [ADP][Pi]/[ATP] = Kcoupled/KG = 1200/(0.00315 M1) = 3.8 105 (M)
GATP = RTlnKATP
= 1.9872 cal mol1 K1 310 K ln(3.8095 105) = 7.9 kcal mol1
33. pH = log10[H+] = log10[103] = (3) = 3
34. pH = log10[H+], so [H+] = 10pH = 106 = 1 M
35. Molality is approximately the same as molarity for dilute solutions. I = 0.5(zi2Mi)
= 0.5[zMn2 (0.35) + zCl2 (0.7)] = 0.5[4 0.35 + 1 0.7] = 1.05
36. Ka = [CH3COO][H+]/[CH3COOH] = [CH3COO][H+]/0.01 = 1.8 105
[CH3COO][H+] = 1.8 107
[CH3COO] = [H+] = (1.8 107)1/2 = 4.2 104
I = 0.5[zacetate2 (4.2 104) + zhydronium2 (4.2 104)] = 0.5[2 (1 4.2 104)]
= 4.2 104
37. Assume that the temperature is 25 C.
a) 5 mM H2SO4
I = 0.5[zsulfate2 (5 103) + zhydronium2 (2 5 103)] = 0.5[(4 + 2) (5 103)]
= 1.5 102
This calculation assumes complete dissociation of the acid (a reasonable
approximate). Moreover, it does not include the ionization of water. The
contribution, however, of hydroxyl ions and hydronium ions to the ionic strength,
is negligible.
logi = Hzi2I0.5
logsulfate = 0.509(22)I0.5 = 0.509 4 (1.5 102)2 = 4.581 104
sulfate = 10(0.0004581) = 0.9989
loghydronium = 0.509(12)I0.5 = 0.509 1 (1.5 102)2 = 1.145 104
sulfate = 10(0.0001145) = 0.9997
b) 2 mM NaCl

2001-2007 by D.T. Haynie. All rights reserved.

I = 0.5[zNa2 (2 103) + zCl2 (2 103)] = 2 103

logNa = 0.509(12)I0.5 = 0.509 1 (2 103)2 = 2.036 106
Na = 10(0.000002036) = 0.999995
Cl = 0.999995
At low ionic strength, 1.
38. The experimental data, when plotted, appear as shown in the figure. The first
column of numbers represents log(x/(co-x)), where x is the equivalents of OH
added, and co is the equivalents of HA initially present. At the isoelectric point,
the equivalents of OH added is 0.5, and one has log(0.5/(1-0.5)) = 0. At more
acidic pH, however, the logarithm is less than zero, because the numerator is
smaller than the denominator. The stronger the base, the lower the pH at which 50
% dissociation occurs.
So, oxyhemoglobin is a better acid than
deoxyhemoglobin.

39. The greater the energy (heat) liberated during a reaction, the greater the affinity of
the reactants for each other. As we have seen in Chapter 2, such reactions are
exothermic; H < 0. Exothermic reactions are thermodynamically favourable at
constant temperature and pressure because G = H TS. The example of water
freezing, however, shows that H alone does not predict the direction of
spontaneous change. A spontaneous reaction can indeed have H > 0, which on
its own would be unfavorable, but only if S > 0 and TS > H. As we shall see

2001-2007 by D.T. Haynie. All rights reserved.

in later chapters, the binding of one molecule to another, for example a hormone
ligand to a membrane-bound receptor, can be described in terms of thermodynamic
quantities. One type of ligand binds a certain type of receptor with high affinity,
another type of ligands binds the same receptor with low affinity. What is meant
here, however, is not the enthalpy change of binding, but the free energy change,
and as we have seen a negative free energy change can involve an increase in
enthalpy.
40. In solution thermodynamics, H H except at very high concentrations of
solute, when solute-solute interactions are no longer negligible. Moreover, in
many cases H is approximately independent of temperature (but not for protein
denaturation!). G is very different: it is highly dependent on temperature and
concentration.
41. The Henderson-Hasselbalch equation tells us that
pH = pKa log([HA]/[A])
Rearranging to solve for the argument of the logarithm, we have
[HA]/[A] = 10(pKa pH) = 1041 = 1000
There are 1000 HAs for each A at pH 1, so the percentage ionized is 0.1 %.
42. Tris can be used in scanning calorimetry experiments, but it is generally advisable
to avoid it if possible. Why should that be, if the heat capacity of a protein
solution is always measured relative to pure buffer in a differential scanning
calorimeter? If the buffer is gaining or losing protons during the experiment, the
pH of solution is changing, and this could have dramatic consequences for protein
stability (Chapter 2). In the ideal case, a DSC experiment will measure the effect
of changing one variable only: the temperature.
pH = pKa log([Tris+]/[Tris])
Rearranging to solve for the argument of the logarithm, we have
[Tris+]/[Tris] = 10(logKa pH) = 10(log(8.3 nM) 8.0) = 10(0.0809) = 1.2
There are about six Tris+ ions for every five Tris molecules.
If the total concentration of Tris is 150 mM, then [Tris+] + [Tris] = 150 mM. We
have two unknowns, but a unique determination of them can be made because we
have two independent relationships involving them. Combining these gives
1.2[Tris] + [Tris] = 2.2[Tris] = 150 mM
from which [Tris] = 68 mM and [Tris+] = 82 mM
The increase in number of dissociated protons increases the driving force for
protonation of Tris. The number of protons that become bound to Tris is the same

2001-2007 by D.T. Haynie. All rights reserved.

as the decrease in the number of unionized Tris molecules and the decrease in
number of free protons, assuming that all H+ from the added HCl binds to Tris
(which is approximately correct).
We assume complete dissociation of HCl.
concentration of 10 mM,

After addition of the acid to a

[Tris] = 58 mM and [Tris+] = 92 mM

By the Henderson-Hasselbalch equation,
pH = pKa log([Tris+]/[Tris]) = log(8.3 109) log(92/58) = 7.9
This is a reduction in pH by about 0.1 units.
If the total concentration of Tris is reduced to 30 mM, then [Tris+] + [Tris] = 30
mM. This is a 5 dilution of the original solution.
1.2[Tris] + [Tris] = 2.2[Tris] = 30 mM
from which [Tris] = 14 mM and [Tris+] = 16 mM
After addition of 5 mM HCl,
[Tris] = 9 mM and [Tris+] = 21 mM
The pH is:
pH = pKa log([Tris+]/[Tris]) = log(8.3 109) log(21.36/8.63) = 7.7
This is a reduction in pH by about 0.3 units. The buffering capacity of a buffer
depends on its concentration.
43. [creatineu] 40[creatines]
= + RTln[creatine]
The transfer is from blood to urine, so
= u s = u + RTln[creatine]u (s + RTln[creatine]s)
= (u s) + RT(ln[creatine]u ln[creatine]s)
= (u s) + RTln([creatine]u/[creatine]s)
We assume that the standard state free energy of creatine does not depend on
whether it is in urine or serum. This is not a bad approximation because creatine is
soluble and the concentration of water is high in urine and serum. So we are left
with
= RTln([creatine]u/[creatine]s) RTln(40) 1.9872 cal mol1 K1 310 K

2001-2007 by D.T. Haynie. All rights reserved.

 2.3 kcal mol1

44. A biochemical redox reaction will be spontaneous (under standard state
conditions) if V' > 0. But the reduced form of molecules in couples with
negative reducing potentials are strong reducing agents, or reductants. Thus, the
strongest reducing agent of the redox pairs shown in ferrodoxin. This protein,
which is found in the stroma of chloroplasts, plays a key role in the light-driven
transport of electrons in photosynthesis (Chapter 5).

2001-2007 by D.T. Haynie. All rights reserved.