The Energetics of Life

Thermodynamic of catalysis
SHAZILAH KAMARUDDIN
[email protected]
 Relationship between DG, DH and DS

D G = D H - TD S
A reaction is favorable when DG is negative.

An increase in entropy (+DS) or a release of heat

(-DH) make DG more negative and are typical of
favorable reactions.
 Biochemists Definitions

DGº - standard free energy change

DGº is the driving force toward equilibrium when reactants
and products are at 1 M concentrations at 298 K (25ºC).

DGo - Biochemists standard free energy change

DGo is the standard free energy change when pH = 7 and the
concentration of H2O is assumed to be constant
at 55.5 M.
 DGo DGo’ for biochemical reactions

In vitro standard conditions = 25oC, 1 atm, 1M

In vivo standard conditions = 25oC, 1 atm, [H+] = 10-7 M

— DG = DG0 + RT In [ product ] @ std conditions

[ reactant ] in vitro

— DG = DG0’ + RT In [ product ] @ std conditions

[ reactant ] in vivo
 Consider the following reaction:

aA + bB ßà cC + dD

The equilibrium constant is given by:

[C]c[D]d
Keq =
[A]a[B]b
When the reaction is not at equilibrium there is a force
driving the reaction to equilibrium. This force is
represented by DG.
 AT EQUILIBRIUM DG = 0

For the reaction reactant product @ equilibrium:

— DG = DG0’ + RT In [ product ] @ std conditions in vivo

[ reactant ]
becomes;

— DG0’ = - RT In [ product ]@ equilibrium

[reactant ]@ equilibrium
[ product ]@ equilibrium = Keq
[ reactant ]@ equilibrium
 Biochemistry Uses ΔGo Not ΔGo
Standard Conditions (all reactants and products at 1M, gases
at 1 atm, Temp = 25C) are Not Biological Conditions

So, [H+] is set at pH 7 (not 1M which would be pH=0)

and for humans uses 37oC (310 K), but for bacteria
uses 25oC (298 K)….or the temperature of the environment.

ΔGo = - RT ln Keq
becomes;
DG0’ = - RT ln Keq = - 2.303 RT log Keq
R = 8.314 J mol-1 K-1 or 0.008314 kJ mol-1 K-1.
T is the temperature on the Kelvin scale.
Keq is determined by letting in vitro reaction reach
equilibrium & determining [ product ] & [ reactant ] @ equilibrium

DG0’ may be calculated if Keq is known

—Negative DG0’ value indicates that @ 25oC, 1 atm,

[H+] = 10-7 M (in vivo std conditions), formation of
product is favored
 Example of Calculation of DG0’

For the reaction : glu-1-phosphate glu-6 phosphate

catalyzed by phosphoglucomutase:

[glu-6-phosphate ] = [glu-1-phosphate ] = 20 mM @ start &

allowed to reach equilibrium

[glu-6-phosphate ]@ equilibrium = 19 mM
[glu-1-phosphate ]@ equilibrium = 1 mM
\ Keq= 19 mM = 19
1 mM
DG0’ = - 2.303 RT log 19 = - 7.3 kJ mol-1
 For the reaction A + B C + D:
Negative DG0’ value indicates direction of rxn. :
Zero DG0’ value indicates rxn is at equilibrium:
Positive DG0’ value indicates direction of rxn. :

Example: for glu-1-phosphate glu-6-phosphate

DGo’ = - 7.3 kJ mol-1

— Direction of reaction:
— Favours formation of glu-6-phosphate
— Exergonic
DG0’ FOR ATP HYDROLYSIS: Does ATP
Hydrolysis is spontaneous process or not?

ATP + H2O ADP + Pi

Keq = [ ADP][Pi ] = 2.23 X 105
[ATP]

DG0’ = - 2.303 RT log Keq

DG0’ = - 2.303 (8.31 J) (298oK) log 2.23 X 105

moloK
= - 30.5 kJ
mol
 RELATIONSHIP BETWEEN Keq & DG0’

Keq DGo’

0.001 17.1
@ Keq <1.0, DG0’ becomes
0.01 11.4 increasingly positive
(endergonic)
0.1 5.7

1.0 0.0 @ Keq = 1.0, DG0’ = 0

10.0 -5.7

100.0 -11.4
@ Keq > 1.0, DG0’
becomes increasingly
1000.0 -17.1 negative (exergonic)
Free energy, or the equilibrium constant, measure
the direction of processes
 Free energy in metabolic
reactions
— Metabolism
— Collection of biochemical reactions that occur within a
cell

— Metabolic pathways
— A group of reactions
— Sequence of chemical reactions

— Two reactions/pathways:
— Catabolic reactions/pathways
— Anabolic reactions/pathways
 Free energy in metabolic
reactions
Catabolic Anabolic
reactions/pathways reactions/pathways
— Disassembly of more — Synthesis of more complex
complex molecules to form compounds
simpler products
— Energy requiring
— Provide chemical energy in
the forms of high-energy
phosphate (ATP) and high-
energy electrons (NADPH)
 Bioenergetics and Reactions

— Thermodynamics applies to biochemistry

— Biological systems utilize free energy and molecular building blocks to
grow, to reproduce & to maintain dynamic homeostasis
— Some biomolecules are high energy with respect to their hydrolysis and
group transfers à ATP
 ENERGY FROM EXTERNAL SOURCES ARE
TRANSFORMED TO GENERATE ATP

— Generation of ATP involves transformations of energy

obtained from outside the cells

— Solar energy & energy obtained from food nutrients

need to be transformed into a form useable by the
cells

— Energy transformations obey the first & second laws of

thermodynamics
 ATP: Adenosine Triphosphate
All living organisms, from bacteria, fungi, spinach and worms to crocodiles and humans, use
ATP for energy conversion.

Originally, the energy comes from the sun.

Plants capture it during photosynthesis and convert it to chemical energy as ATP. Using this
energy, plants produce carbohydrates, fats and proteins which are eaten by animals and
human beings.

In metabolism, the food is broken down and the energy released is used to make ATP.

Energy is interconverted between various forms. Compare this with the idea of different
currencies, only one of which is accepted at a time. ATP is an energy currency.
 ATP CONTAINS FREE ENERGY

Free energy (G) ATP º a form of energy useable in

biological systems

ATP hydrolysis is accompanied by a free energy

change of -30.5 kJ/mol

ATP is continuously used & formed (adults require

»40 kg ATP per day and the requirement increases
with exercise or strenuous activity)
 Life's energy currency, ATP

Cooper GM. The Cell: A Molecular Approach. 2nd edition.

Sunderland (MA): Sinauer Associates; 2000. Metabolic
Energy.

Highly exergonic process

The bonds between the phosphate groups of ATP are called high-energy bonds because their
hydrolysis results in a large decrease in free energy. ATP can be hydrolyzed either to ADP plus
a phosphate group (HPO42-) or to AMP plus pyrophosphate. In the latter case, pyrophosphate
is itself rapidly hydrolyzed, releasing additional free energy.
 Coupling endergonic and exergonic processes

Reactions with large positive DG˚’ values are ‘driven’ by input of energy

— Glucose + Phosphate (HPO42-) ® Glucose-6-phosphate + H2O

(DG˚’= +3.3 kcal/mol) à this reaction is energetically unfavorable

Thus, it must be driven in the forward direction by being coupled to ATP

hydrolysis

— ATP+ H2O ® ADP + HPO42- (DG˚’ = -7.3 kcal/mol)

— The combined reaction can be written as follows:

— Glucose + ATP+ H2O ® Glucose-6-phosphate + ADP (DG˚’ = -4.0 kcal/mol)

— energetically favoring glucose-6-phosphate formation
The high-energy bonds of ATP thus play a central role in cell metabolism by serving as a
usable storage form of free energy.
 Activation Energy
— All reactions, both endergonic and exergonic, require an input of energy called
activation energy (EA)to get started.

— Is the initial amount of energy needed to start a chemical reaction

— Activation energy is needed to bring the reactants close together and weaken
existing bonds to initiate a chemical reaction.

A B

C D

Transition state

A B EA
Free energy

C D

Reactants
A B
∆G < O
C D

Products

Progress of the reaction

Copyright © The McGraw-Hill Companies, Inc. Permission required for reproduction or display.
 Overcome activation energy
barrier
1. Increased energy content of all molecules
— Increasing the average energy content by input of
heat

2. Lowering the activation energy

— By a CATALYSTS that enhances the rate of reaction

— Enzymes speed up the rate of a biochemical reaction by lowering the

activation energy
— When an enzyme binds to a substrate it stresses and destabilises the
bonds in the substrate
— This reduces the overall energy level of the substrate’s transitionary
state, meaning less energy is needed to convert it into a product and
the reaction proceeds at a faster rate
 Enzymes Lower the EA Barrier
— An enzyme catalyzes reactions by lowering the EA barrier

Course of
reaction EA
without
without
enzyme
enzyme
EA with
enzyme
is lower
Free energy

Reactants

Course of ∆G is unaffected
reaction by enzyme
with enzyme

Products

Progress of the reaction

 Activation energy (EA)

http://ib.bioninja.com.au/higher-level/topic-8-metabolism-cell/untitled-6/activation-energy.html
 Cruel fate of Antoine Lavoisier
• French nobleman and chemist who was central to the
18th-century chemical revolution
• Had a large influence on both the history of chemistry and
the history of biology.
• From a medical point of view, he introduced the study of
respiration and metabolism and so founded
biochemistry.
• He is widely considered in popular literature as the "father
of modern chemistry".
• one of the first to execute and exploit quantitative
research through his experiments.
• Lavoisier’s final fate was cruel. During the French
revolution he was sentenced to death for his political and
economic views. Prior to being executed, he asked the
judge for permission to complete his scientific research,
first. He was guillotined for these accusations in Paris on
the 8th of May 1794, fifty years old, and sadly the world
lost one of the greatest scientists and researchers.
The End