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Bioenergetics Learning Objectives

This document outlines learning objectives for understanding bioenergetics and the role of ATP. It discusses: 1) The first and second laws of thermodynamics as they apply to biochemical reactions, including the concept of entropy, enthalpy, and free energy. 2) How the Gibbs free energy equation (ΔG = ΔH - TΔS) can be used to determine if a reaction is spontaneous or favors a particular direction. 3) How endergonic reactions can be driven by coupling to exergonic reactions through the use of ATP and other high-energy phosphates in biological systems. 4) The role of ATP and other nucleotide triphosphates as the "energy

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María Valle Rodríguez
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172 views

Bioenergetics Learning Objectives

This document outlines learning objectives for understanding bioenergetics and the role of ATP. It discusses: 1) The first and second laws of thermodynamics as they apply to biochemical reactions, including the concept of entropy, enthalpy, and free energy. 2) How the Gibbs free energy equation (ΔG = ΔH - TΔS) can be used to determine if a reaction is spontaneous or favors a particular direction. 3) How endergonic reactions can be driven by coupling to exergonic reactions through the use of ATP and other high-energy phosphates in biological systems. 4) The role of ATP and other nucleotide triphosphates as the "energy

Uploaded by

María Valle Rodríguez
Copyright
© © All Rights Reserved
Available Formats
Download as DOCX, PDF, TXT or read online on Scribd
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Learning Objectives for Chapter 11: Bioenergetics: The

Role of ATP

1. Define and explain briefly the role of entropy and


enthalpy in biochemical reactions

Biologic Systems conform to the general laws of


thermodynamics.

The first law of thermodynamic states that the total energy of


a system, including its surroundings,remains constant. In all
living systems, chemical energy is 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 a disorder or
randomness of the system and becomes maximum as
equilibrium is approached.

2. Apply the Gibbs free energy equation to determine


reaction favorability and explain coupled reactions.

Under a constant temperature and pressure, the relationship


between free energy change (G)ofareactingsystemandthe
changeinentropy(S)isexpressedbytheequationGHTS.
whereHisthechangeinenthalpy(heat)andTistheabsolute
temperature.

Inbiochemicalreactions,becauseHisapproximatelyequaltoE,the
totalchangeininternalenergyofthereaction,theaboverelationship
maybeexpressedinthefollowingway:

G = E - TS

If G is negative, the reaction proceeds spontaneously with


loss of free energy; ie, it is exergonic. 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 posi-
tive, the reaction proceeds only if free energy can be gained;
ie, 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 G is zero, the system is at equilibrium
and no net change takes place.
3. State the first and second laws of thermodynamics and
understand how they apply to biological systems.

The first law of thermodynamic states that the total


energy of a system, including its surroundings,remains
constant. In all living systems, chemical energy is
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 a disorder
or randomness of the system and becomes maximum as
equilibrium is approached.

Under conditions of constant temperature and pressure, the


relationshipbetweenthefreeenergychange(G)ofareacting
system and the change in entropy (S) is expressed by the
following equation, which combines the two laws of
thermodynamics:

GHTS(GibbsEquation)

where H is the change in enthalpy (heat) and T is the


absolute temperature.

How does it apply to biochemical reactions? 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:

G = E - TS

If G is negative, the reaction proceeds spontaneously


with loss of free energy; ie, it is exergonic. 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 posi- tive, the reaction proceeds
only if free energy can be gained; ie, 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 G 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, G0 is the standard free-energy change. For
biochemicalreactions,astandardstateisdefinedashavingapH
of7.0.Thestandardfreeenergychangeatthisstandardstateis
denotedbyG0.

The standard freeenergy change can be calculated from the


equilibriumconstantKeq.

G0RTlnKeq

whereRisthegasconstantandTistheabsolutetemperature.It
isimportanttonotethattheactualGmaybelargerorsmaller
than G0 depending on the concentrations of the various
reactants,includingthesolvent,variousions,andproteins.

In a biochemical system, an enzyme only speeds up the


attainmentofequilibrium;itneveraltersthefinalconcentrations
ofthereactantsatequilibrium.

4. Explain what is meant by the terms free energy, entropy,


enthalpy, exergonic, endergonic, endothermic, and
exothermic.
Free energy
Entropy
Enthalpy
Exergonic
Endergonic
Endothermic
Exothermic
5. Appreciate how reactions that are endergonic may be driven
by coupling to those that are exergonic in biologic systems.
6. Understand the role of high-energy phosphates, ATP, and
other nucleotide triphosphates in the transfer of free energy
from exergonic to endergonic processes, enabling them to act
as the energy currency of cells.

Easy Resources for better understanding links Q&A:


Link #1:
1. How much of the cytoplasmic volume do proteins take
up?

They take up to 40% of the cytoplasmic volume creating a


molecular crowdy?

2. What situation is the result?

That creates a molecular cluster that increases the protein


aggregation between hydrophobic patches and unfolded regions of
proteins.

3. What mechanism is in place to address protein


aggregation?

Targeted degradation by proteasomes normally limits the


consequences of protein aggregation. So not all proteins fuse
freely ???***

4. What is the function of vesicles?


Vesicles

5. What is the function of kinesin, a motor protein?

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