Chapter 13

Principles of
Bioenergetics
Bioenergetics : the quantitative study of
energy transductions in living cells and
the physical-chemical nature underlying
these processes.

The bioenergetics has been

studied since the time of
Antoine Lavoisier

Animal respiration was considered as a slow

combustion of carbon and hydrogen, with O2
consumed, CO2 and H2O produced, similar to
what occurs in a candle (1790s, Lavoisier).
CO2 production was observed in insects, a
variety of animal tissues and plants in the
dark (1790s to 1840s).
Two general questions: where O2 is converted
to CO2 and H2O in animals? In what form
does the carbon and hydrogen exist?

The bioenergetics has been

studied since the time of
Antoine Lavoisier

The O2 to CO2 conversion was initially

considered to occur in the lungs, then in the
blood, then in all tissues (e.g., muscle).
Fats and carbohydrates were considered as
the fuel of the animal body (Liebig, 1840s).
The role of hemoglobin in reversibly binding
O2 became clear in the 1860s.
The application of thermochemistry and
thermodynamics in studying bioenergetics:
heat was considered a major form of energy in
animals for a long time.

Cells need energy to do all

their work

To generate and maintain its highly ordered

structure (biosynthesis of macromolecules).
To generate motion (mechanical work).
To generate concentration and electrical gradients
across cell membranes (active transport).
To generate heat and light.
The energy industry(production, storage and
use) is central to the economy of the cell society!

Cells have to use chemical

energy to do all their work

Living cells are generally held at constant

temperature and pressure: chemical energy
(free energy, G) has to be used by living
organisms.
Biological energy transformation obey the
two basic laws of thermodynamics.
The free energy concept of thermodynamic
is more important to biochemists than to
chemists

describe energy changes

occurring in a chemical
reaction

G = G'o + RT ln Q (Q = [products]/[reactants])
G' o = -RT ln K'eq (K'eq : equilibrium constant)
The actual free energy change (G ) determines
whether a reaction occurs spontaneously.
The standard free energy change in biochemistry
( G'o) is a constant (measured under a standard
set of conditions).
G for a reaction can be larger, smaller, or the
same as G'o, depending on the concentrations of
the reactants and products (Q: mass action ratio).

The G and G'o values are additive when

reactions are coupled, thus a
thermodynamically unfavorable reaction can
be driven by a favorable one.
The overall K`eq is multiplicative (the product
of two, ), although G'o is additive
(the algebraic sum of two ).
Note: the rate of a chemical reaction has
nothing to do with its G or G'o, but is
determined by its activation energy (G )!

ATP is the universal

currency for biological
energy

This was first perceived by Fritz Lipmann and

Herman Kalckar in 1941 when studying glycolysis.
Hydrolysis of the two phosphoanhydride (
) bonds in ATP generate more stable products
releasing large amount of free energy ( G'o is
-30.5 kJ/mol; Gp in cells is -50 to -65 kJ/mol).
The ATP molecule is kinetically stable at pH 7 and
enzyme catalysis is needed for its hydrolysis.
ATP actually exists as a sum of various species in
cells (e.g., ATP4- and MgATP2-).

Fig. 2. The two-dimensional stick model of the adenosine phosphate family of molecules, showing the atom and bond
arrangement.

ATP provides
energy usually
through group
Gln synthetase

transfer
(protein could
also be such
acceptors)

Nucleophilic attacks
Not phosphate

ATP usually provides energy by group transfer of

phosphoryl groups ( ), not phosphate groups;

rming covalent intermediates), not by simple hydroly

ATP has an intermediate phosphoryl group

transfer potential, thus ADP can accept and
ATP can donate phosphoryl groups (forming
the ATP-ADP cycle and acting as an energy

ATP is not a long-term storage form of free energy

living cells, but phosphocreatine is one such phosp
reservoir, or so-called phosphagen.

oxidation-reduction
reactions generates
biological energy
H2O

O2
Free energyTransmembrane
Proton gradient

2e

2e

2e

Metabolic fuels

Oxidation

ATP

(NADH, FADH2)

2e-

CO2

Metabolic fuels are oxidized to CO2, with electrons

transferred first to universal carriers (e.g., NAD + and FAD),
and eventually to O2.
Energy is released during such redox reactions and
eventually conserved in ATP.

Carbons in the metabolic fuels will

keep losing pairs of electrons (carried
by hydrogen) in the stepwise oxidation
process, and eventually be lost as CO2
in which the carbon does not own
any electrons (i.e., with electrons
completely extracted.
The more electronegative atom owns
the bonding electrons it shares with
another atom.

Electronegativity: H < C < O

Carbon owns different numbers of electrons in its various

oxidation states.

5
8

2
4
7

2
3

1
0

of an redox
reaction is
particularly
easy to
determine

e-

It can be determined
simply by measuring
the voltage difference
between the two halfcells, with each
containing a halfreaction of the redox
reaction.

Reduction potentials (E) are defined

with respect to an arbitrary standard

Standard reduction potential (E'o) of each oxidant

is measured by connecting a test half-cell
having the oxidized and reduced species of the
redox pair each at 1 M, or 1 atm for gases, pH 7
to a reference half-cell having 1 M H+ and 1 atm
H2, whose E' o is arbitrarily assigned as 0.00 V.

By convention, the redox pair having a higher

tendency to acquire electrons is given a positive
value of E'o.

Measuring the standard

reduction potential (E'o)

e-

pH 0
pH 7
E' o = 0.00 V positive E'

e-

E'

pH 0
= 0.00 V

pH 7
Negative E'

G can be calculated via E

G of a redox reaction can be directly

calculated from the value of E (= E

of the electron acceptor E of the

electron donor):

When E is positive, G is negative.

(E) of each half-reaction can be

calculated according to the
Nernst equation

The actual reduction potential (E')

depends on the standard reduction
potential (E'o ), electrons transferred per
molecule (n), temperature (T), ratio of
[reduced form]/[oxidized form]:
E'

E'

[oxidized form]
[reduced form]

NAD is a widely occurring electron

carrier

NAD+ (Nicotinamide Adenine Dinucleotide)

reversibly accepts an hydride ion (an
equivalent of two electrons and one proton)
at the nicotinamide portion;
Reduction of the nicotinamide ring produces
a new, broad absorption band with a
maximum at 340 nm.

NAD+ is a cofactor of many

dehydrogenases, whose action can
be
conveniently followed by observing

carrier

FAD (Flavin Adenine Dinucleotide) is able to

accept/donates one or two electrons
(as hydrogen atom) each time.
It is usually tightly bound to the dehydrogena
(also called flavoproteins), which are often
complex and contain other inorganic ions to
help the electron transferring process.

The vitamins niacin (nicotinic acid)

and riboflavin (vitamin B2) provide
precursors for making NAD/NADP
and FAD/FMN

Niacin

Riboflavin

NAD+

FAD

Summary

Bioenergy is chemical energy, studied in terms of

free energy and free energy change (G ).
ATP acts as the free energy carrier (currency) in cells.
Bioenergy is mainly produced via stepwise electron
flow (redox reactions) through a series of electron
carriers having increasing levels of reduction
potential (E).
Electrons released from the oxidation of nutrient fuels
are initially channeled to a few universal electron
carriers (including NADH and FADH2).