Bioenergetics Course - 2004 - Lecture 3a, review of thermodynamics        

Keith D. Garlid            April 16, 2004





ENERGY UNITS AND CONVERSION FACTORS


Here are some common constants used in bioenergetic calculations:

F = 96,487 coul / equiv   (The Faraday)

R = 8.314 joules / deg (The Gas Constant)

RT/F = 25.688 at 25 oC

Following is a brief review of the origin of these units, for your information.

newton (N)

The newton is the Standard International (SI) unit of force.  One newton is the force required to cause a mass of one kilogram to accelerate at a rate of one meter per second squared in the absence of other force-producing effects.  Force (F) in newtons, mass (m) in kilograms, and acceleration (a) in meters per second squared are related by a formula well known in physics:

    F = ma

joule (J)

When objects interact, i.e. exert forces on each other, then the work exerted by one object on another is defined as

   Work = Force x Distance

One joule is defined as the amount of energy exerted when a force of one newton is applied over a displacement of one meter.  (One joule is the equivalent of one watt of power radiated or dissipated for one second.)

Energy

The work done by an object is exactly equal to the loss in energy that the object experiences while doing that work.  It is also equal to the energy that the object being acted on gains. This discovery (the conservation of energy) is called the "work-energy theorem" in physics.  Note that this means that Energy must have the same units as Work, i.e., the joule.

Calories
 
The calorie is defined as the amount of heat needed to raise the temperature of 1 gram of water by 1C .  But this makes the calorie depend on the initial temperature of the water.  Recall that heat is a form of energy, so it can also be quantified by the joule.  The joule is superior because it is independent of temperature.  

    We may take 1 kcal (1000 cal) = 4.184 kJ


Voltage (V)

Voltage, also called electromotive force, is a quantitative expression of the potential difference in charge between two points in an electrical field. The greater the voltage, the greater the flow of electrical current (that is, the quantity of charge carriers that pass a fixed point per unit of time) through a conducting or semiconducting medium for a given resistance to the flow. The standard unit is the volt.  One volt will drive one coulomb (6.24 x 1018) charge carriers, such as electrons or ions, through a resistance of one ohm in one second.

    A charge (electron or ion) moving through a voltage is a form of work.  Moreover, a charge having the potential to move through a voltage is a form of energy.  The general conversion between electrical force and energy is:

ΔG = znFΔV

where ΔG is in J/mol, z is the valence, n is the number of charges moved, and F is the Faraday:

1 Faraday (F) = 96485.3415 Coulombs

Examples

(a) What is the free energy of an electron falling through 1 volt?

For an electron, n = 1 and z =  - 1, ΔV = 1 volt, so ΔG = 96.485 kJ/mol


(b) Protonmotive force, Δp ~ 200 mV

    Definition: Δp   =   - ΔμH+/F (n = 1, the charge on H+)

    Therevore,  ΔμH+ = - 96.485 x 0.2 V =   - 19.3 kJ/mol
           
(b) Redox energy, ΔE, for NADH to O (2 electrons, z = -1)

    ΔE = -2 x 96.485 x 1.16 =  -216 kJ/mol




GIBBS FREE ENERGY, ΔG, AND CHEMICAL POTENTIAL, Δμ


1.  Gibbs Free Energy, ΔG


Josiah Willard Gibbs introduced the State Function ΔG, which is DEFINED as follows:

ΔG = ΔH  - TΔS

2.  General properties of ΔG:


    1)  A system is at equilibrium if ΔG = 0 (very important)

    2)  A reaction can occur spontaneously ONLY if ΔG is negative.

    3)  A reaction CANNOT occur spontaneously if ΔG is positive.

    4)  ΔG is a STATE function.  Therefore it depends only on the free energy of the products minus the free energy of the reactants.

    5)  ΔG is INDEPENDENT OF THE PATH of the transformation.  (The same whether or not catalyzed by an enzyme)

    6)  ΔG provides no information about the RATE of the reaction


3.  ΔG for a chemical reaction


Consider the chemical reaction

A + B   ⇄ C + D

ΔG = ΔG o   + RT ln   [C][D]
               [A][B]

ΔG o   is the standard free energy change   
R is the gas constant = R = 8.314 joules / deg
T is absolute temperature = 298.14 at 25 oC
[A], [B], [C], [D ] are molar concentrations of reactants and products.

4.  The chemical potentials - μ


G is a function of T, P, and the number of mols of each component:

    G = G(T, P, N1,....Nn)

We will want to know the free energy associated with a given component of the system.  This is called the chemical potential or partial molal free energy and is defined thus:

μj   ≡  (∂G/∂Nj )T,P,Ni

(This partial derivative means:  the derivative of G with respect to quantity, N, of a particular component, holding all other properties constant).

The chemical potential takes the same form as the free energy (because it is a free energy).

μj   =  μj o    +   RT ln cj

where cj is the concentration of species “j”, and  μj o is the standard chemical potential, usually defined as 1 molal.

We are normally interested in differences in μ across the inner membrane.  Because Δμo relates to standard conditions in two (similar) aqeuous phases, we take Δμo = 0.  Therefore,

Δμ   = RT ln c(in)/c(out)

This is the partial molal free energy of moving a solute (nonelectrolyte) from outside to inside.  Note that if c(out) > c(in), Δμ is negative, and the reaction will occur spontaneously.

5.  Electrochemical potentials, Δμ


The electrochemical potential difference for an ion takes into account the electrical energy as well as the chemical energy.  For any ion of valence, z,

Δμ   = RT ln c(in)/c(out) + zF ΔΨ

where ΔΨ refers to the electrical potential difference, inside minus outside. 

6.  Protonmotive force, Δp (mV)


Δp is DEFINED as,

Δp =  - ΔμH+ / F

Therefore,
Δp = Z ΔpH  - ΔΨ

where Z  ≡ RT log(e) / F ~ 59 mV at 25 oC
and ΔpH = pHin  - pHout

Typical measurements in mitochondria respiring on succinate (but not phosphorylating) are: ΔpH ~ 0.3 (alkaline inside), and ΔΨ~ -190 mV (negative inside).  Therefore,
Δp ~ 208 mV.

7.  Chemical reactions at equilibrium - the equilibrium constant, Keq


ΔG = 0 at equilibrium.  From section 3,

go to ATP
ΔGo   =  - RT ln   [C’][D’]
               [A’][B’]

where primes indicate that all concentrations refer to those achieved at equilibrium.  We define the equilibrium constant as

Keq =     [C’][D’],
             [A’][B’]

so ΔGo   =  - RT ln Keq
                 

Keq can, in principle, be measured, allowing calculation of ΔGo and vice versa.  For example, take ΔGo for ATP synthesis to be + 30.6 kJ/mol. 
Then ln Keq = -30.6/(0.008314 x 298.16) =  -12.3442, and Keq ~ 4.36 x 10-6

Nicholls and Ferguson introduce a parameter Γ, to describe the actual concentrations in the free energy equation.  This leads to a simple form:

ΔG = RT ln (Γ /  Keq)

8.  Partitioning of a solute between two phases - the partition coefficient, Kp


It is frequently of interest in biology to know how molecules partition between the aqueous phase and the hydrophobic interior of membranes.  Here, we use the equation given in section 4, but we must include a standard chemical potential change Δμo, because the two phases are different.  Therefore,

Δμ   = Δμo +   RT ln c1/c2

where 1 and 2 refer to the lipid and aqueous phases, respectively.

We allow the solute to come to equilibrium between the two phases, therefore, Δμ = 0, and

Δμo  =  - RT ln c1/c2 = - RT ln Kp

where Kp =   c1/c2

Δμo is referred to as the free energy of transfer of the solute from phase 2 to phase 1.

Note also that another way of writing the equation is,
       

c1/c2   =   e-Δμo/RT


9.  Ions at equilibrium across a membrane - the Nernst potential


From section 5, we may write the equation for the electrochemical potential of K+ across the inner membrane of mitochondria.

ΔμK+   = RT ln [K+]in /[K+]out + F ΔΨ

For mitochondria in vivo, K+(in) ~ K+(out) ~ 140 mM.  Therefore,

ΔμK+   ~  F ΔΨ ~  -19.3 kJ/mol (for ΔΨ = 0.2 V).   This is a very large driving force for inward K+ diffusion!

Experimentally, we may estimate ΔΨ from the K+ equilibrium potential.  It is necessary to lower [K+]out to about 0.14 mM.  We then add valinomycin, a K+ ionophore that catalyzes electrophoretic flux of K+ across the inner membrane, until K+ comes to equilibrium.  Note that mitochondria are respiring, so the system is NOT at equilibrium.  We say that the system is in a state of partial equilibrium with respect to the process of electrophoretic K+ diffusion.  When this is achieved, we know that ΔμK+   = 0.

Therefore, at K+ equilibrium,

Δψeq =    - (RT/F)  ln [K+]in /[K+]out

(NOTE THAT RT/F = 25.688 at 25 oC)

We frequently observe that K+ is taken up until [K+]out ~ 0.1 mM.  Then [K+]in /[K+]out = 1400 (assuming  [K+]in = 140 mM), and ΔΨeq  =  -193 mV.

Note that we can apply the preceding equations to mitochondria with NORMAL K+ concentrations.  We define Δψeq as the hypothetical electrical potential that would obtain if the ACTUAL K+ concentrations were in electochemical equilibrium.  This leads to

ΔμK+   = F(Δψ  -   Δψeq).

Note that, for  [K+]in = [K+]out ,  Δψeq = 0, and once again, ΔμK+   = FΔψ for this case.
This kind of equation is used in describing the biophysics of plasma membrane ion transport, but it is not commonly applied to mitochondria.