Bioenergetics

Bioenergetics
• Bioenergetics, or biochemical thermodynamics, is

the study of the energy changes accompanying
biochemical reactions. Biologic systems are
essentially isothermic and use chemical energy to
power living processes.
• How an animal obtains suitable fuel from its food
to provide this energy is basic to the
understanding of normal nutrition and
metabolism.
FREE ENERGY IS THE USEFUL ENERGY
IN A SYSTEM
• Gibbs change in free energy (∆G) is that
portion of the total energy change in a system
that is available for doing work—i.e., the
useful energy, also known as the chemical
potential
Biologic Systems Conform to the
General Laws of Thermodynamics
• The first law of thermodynamics states that the
total energy of a system, including its
surroundings, remains constant.
• It implies that within the total system, energy is
neither lost nor gained during any change.
• However, energy may be transferred from one
part of the system to another or may be
transformed into another form of energy. In
living systems, chemical energy may be
transformed into heat or into electrical, radiant,
or mechanical energy.
• The second law of thermodynamics states that the
total entropy of a system must increase if a process is
to occur spontaneously. Entropy is the extent of
disorder or randomness of the system and becomes
maximum as equilibrium is approached.
• Under conditions of constant temperature and
pressure, the relationship between the free energy
change (∆G) of a reacting system and the change in
entropy (∆S) is expressed by the following equation,
which combines the two laws of thermodynamics:
• where ∆H is the change in enthalpy(heat) and

T is the absolute temperature. In biochemical
reactions, because ∆H is approximately equal
to ∆E, the total change in internal energy of
the reaction, the above relationship may be
expressed in the following way:
• If ∆G is negative, the reaction proceeds

spontaneously with loss of free energy; ie, it is If,
in addition, ∆G is of great magnitude, the
reaction goes virtually to completion and is
essentially irreversible.
• On the other hand, if ∆G is positive, the reaction
proceeds only if free energy can be gained; i.e., it
is endergonic. If, in addition, the magnitude of
∆G is great, the system is stable, with little or no
tendency for a reaction to occur
If ΔG is zero, the system is at equilibrium and no net
change takes place.
When the reactants are present in concentrations of
1.0 mol/L, ΔG0 is the standard free-energy change.
For biochemical reactions, a standard state is
defined as having a pH of 7.0. The standard free-
energy change at this standard state is denoted by
ΔG0′.
ENDERGONIC PROCESSES PROCEED BY
COUPLING TO EXERGONIC PROCESSES
The vital processes—e.g., synthetic reactions, muscular contraction,
nerve impulse conduction, and active transport—obtain energy by
chemical linkage, or coupling to oxidative reactions.

The exergonic reactions are termed catabolism (generally, the
breakdown or oxidation of fuel molecules),
whereas the synthetic reactions that build up substances are
termed anabolism. The combined catabolic and anabolic
processes constitute metabolism.
Coupling of an exergonic to an
endergonic reaction.
Transfer of free energy from an exergonic to an
endergonic reaction via a high-energy intermediate
compound
HIGH-ENERGY PHOSPHATES PLAY A
CENTRAL ROLE IN ENERGY CAPTURE
AND TRANSFER
• Autotrophic organisms utilize simple endergonic
processes; eg, the energy of sunlight (green
plants), the reaction Fe2+ →Fe3+ (some bacteria).
• Heterotrophic organisms obtain free energy by
coupling their metabolism to the breakdown of
complex organic molecules in their
environment. In all these organisms, ATP plays a
central role in the transference of free energy
from the exergonic to the endergonic processes
ATP is a nucleotide consisting of the nucleoside
adenosine (adenine linked to ribose), and three
phosphate groups in its reactions in the cell.
The Intermediate Value for the Free Energy of
Hydrolysis of ATP Has Important Bioenergetic
Significance
• Low-energy phosphates, exemplified by the ester
phosphates found in the intermediates of
glycolysis, have G0′values smaller than that of
ATP, while in high-energy phosphates the value is
higher than that of ATP.
• The symbol ~ indicates that larger quantity of

free energy. For this reason, the term group
transfer potential, rather than “high-energy
bond”. Thus, ATP contains two high-energy
phosphate groups and ADP contains one,
whereas the phosphate in AMP is of the low
energy type since it is a normal ester link. The
Intermediate Value for the Free Energy of
hydrolysis of ATP has important Bioenergetic
Significance
• The high free-energy change on hydrolysis of
ATP is due to relief of charge repulsion of
adjacent negatively charged oxygen atoms
and to stabilization of the reaction products,
especially phosphate.
Structure of ATP, ADP, and AMP showing the
position and the number of high-energy phosphates
). (~
The free-energy change on hydrolysis of ATP
to ADP.
HIGH-ENERGY PHOSPHATES ACT AS THE “ENERGY
CURRENCY” OF THE CELL
• There are three major sources of ~ P taking
part in energy conservation or energy capture:
• 1. Oxidative phosphorylation
• 2. Glycolysis.
• 3. The citric acid cycle.
role of ATP/ADP cycle in transfer of high-energy
phosphate
When ATP acts as a phosphate donor to form
compounds of lower free energy of hydrolysis, the
phosphate group is invariably converted to one of low
energy. For example, the phosphorylation of glycerol
to form glycerol-3-phosphate
ATP allows the Coupling of

thermodynamically Unfavorable reactions
to Favorable Ones
transfer of high-energy phosphate between ATP and creatine.
adenylate Kinase (Myokinase)
Interconverts adenine Nucleotides
Adenylate kinase is important for the maintenance of energy

homeostasis in cells because it allows:
1. High-energy phosphate in ADP to be used in the synthesis
of ATP.
2. The AMP formed as a consequence of activating reactions
involving ATP to dephosphorylated to ADP.
3. AMP to increase in concentration when ATP becomes
depleted so that it is able to act as a metabolic (allosteric)
signal to increase the rate of catabolic reactions, which in turn
lead to the generation of more ATP
When ATP Forms AMP, Inorganic
pyrophosphate (ppi) Is produced
This reaction is accompanied by loss of free energy as
heat, which ensures that the activation reaction will
go to the right, and is further aided by the hydrolytic
splitting of Ppi catalyzed by inorganic
pyrophosphatase, a reaction that itself has a large ΔG 0
of- 19.2 kJ/mol
phosphate cycles and interchange of adenine
nucleotides.
Other nucleoside
Triphosphates participate in
the Transfer of high Energy
phosphate
By means of the nucleoside diphosphate (NDP)

kinases,UTP, GTP, and CTP can be synthesized from
their diphosphates, for example, UDP reacts with ATP
to form UTP.

Bioenergetics

Uploaded by

Copyright:

Available Formats

Bioenergetics

Uploaded by

Document Information

Copyright

Available Formats

Share this document

Share or Embed Document

Sharing Options

Did you find this document useful?

Is this content inappropriate?

Copyright:

Available Formats

Bioenergetics

Uploaded by

Copyright:

Available Formats

Bioenergetics

• Bioenergetics, or biochemical thermodynamics, is

• where ∆H is the change in enthalpy(heat) and

• If ∆G is negative, the reaction proceeds

chemical linkage, or coupling to oxidative reactions.

• The symbol ~ indicates that larger quantity of

ATP allows the Coupling of

Adenylate kinase is important for the maintenance of energy

By means of the nucleoside diphosphate (NDP)

You might also like