Mary K.

Campbell
Shawn O. Farrell
international.cengage.com/

Chapter Fifteen
The Importance of Energy Changes and
Electron Transfer in Metabolism

Paul D. Adams • University of Arkansas

Standard States for Free-Energy Changes
• Standard states
• for pure solids and liquids, the pure substance
• for gases, the gas at a pressure of 1 atm
• for solutions, a concentration of 1 mol/L
• For the reaction

We can rewrite the equation that relates the G for

the reaction under any conditions to the free-energy
change under standard conditions (G˚)
A Modified Standard State for Biochemical
Applications
• Standard free energy change, G°, assumes a
concentration of 1 M
• if [H+] = 1 M, then pH = 0
• but the pH in most cells is near the neutral range
• For biochemical reactions, we define a different
standard state for the concentration of H+
• standard state for [H+] = 10-7 M, pH = 7.0
• this modified standard state is given the symbol G°’
• Summary
The usual thermodynamic standard state implies that
the system involved is at pH=0, which is seldom, if
ever, found in living things. The modified standard
state explicitly states that the system is at pH=7
Biochemical Connections: Thermodynamics
The Nature of Metabolism
• Metabolism: the chemical reactions of
biomolecules. It is the biochemical basis of life
processes
• catabolism: the breakdown of larger molecules into
smaller ones; an oxidative process that releases
energy
• anabolism: the synthesis of larger molecules from
smaller ones; a reductive process that requires energy
A Comparison of Catabolism and
Anabolism
• Metabolism is the sum total of the chemical reactions
of biomolecules in an organism
The Role of Oxidation and Reduction in
Metabolism
• Oxidation-Reduction reactions are those in which
electrons are transferred from a donor to an acceptor
• oxidation: the loss of electrons; the substance that
loses the electrons is called a reducing agent
• reduction: the gain of electrons; the substance that
gains the electrons is called an oxidizing agent
• Carbon in most reduced form- alkane
• Carbon in most oxidized form- CO2 (final product of
catabolism
Standard States for Free-Energy Changes
(Cont’d)
• When the reaction is at equilibrium, G = 0

• If we can determine the concentration of reactants

and products at equilibrium, we can determine Keq
and, from it, the change in free energy for conversion
of one mole of reactant to product(s)
Summary
• In catabolism, large molecules are broken down to
smaller products, releasing energy and transferring
electrons to acceptor molecules of various sorts. The
overall process is one of oxidation.

• In anabolism, small molecules react to give rise to

larger ones; this process requires energy and
involves acceptance of electrons from a variety of
donors. The overall process is one of reduction
Coenzymes used in Biologically important
Redox Reactions
• Conversion of ethanol to acetaldehyde is a two-
electron oxidation
NAD+/NADH: An Important Coenzyme
• Nicotinamide adenine dinucleotide (NAD+) is an
important coenzyme
• Acts as a biological oxidizing agent
• The structure of NADH is comprised of a
nicotinamide portion. It is involved in the reaction. It
is a derivative of nicotinic acid
• NAD+ is a two-electron oxidizing agent, and is
reduced to NADH
The Structures and Redox States of the
Nicotinamide Coenzymes
FAD/FADH2
• Flavin adenine dinucleotide (FAD) is also a biological
oxidizing agent
• Protons, as well as, electrons are accepted by FAD
The Structures of Riboflavin, Flavin Mono-
nucleotide (FMN), and Flavin Dinucleotide (FAD)
Coupling of Production and Use of Energy
• The coupling of energy-producing and energy-
requiring reactions is a central theme in the
metabolism of all organisms
• Energy cannot be used directly, must by shuttled into
easily accessible forms of chemical energy
• “High Energy” bonds- bonds that require or
release convenient amounts of energy, depending
on the direction of the reaction
• ATP is essential high energy bond-containing
compound
• Phosphorylation of ADP to ATP requires energy
• Hydrolysis of ATP to ADP releases energy
The Phosphoric Anhydride Bonds in ATP
are “High Energy” Bonds
ATP
• 4 (-) charges on ATP and 3 on ADP, therefore ATP
is less stable.
• Why is ATP less stable, charge-wise, than ADP?
• Energy must be expended to put on additional
negative charge on ADP
• Also, entropy loss when ADP is phosphorylated
because there is a potential loss of resonance
hybridization of inorganic phosphate (Pi) upon
phosphorylation of ADP to ATP
Loss of a Resonance-Stabilized Phosphate
Ion in Production of ATP
ATP Hydrolysis Decreases in Electrostatic
Repulsion
• Marked decrease in
electrostatic repulsion
of -phosphate of
GDP upon hydrolysis of
ATP to ADP
Organophosphates Important in Producing
Energy
Role of ATP as Energy Currency
Summary
• Hydrolysis of ATP to ADP releases energy

• In the coupling of biochemical reactions, the energy

released by one reaction, such as ATP hydrolysis,
provides energy for another
Coenzyme A in Activation of Metabolic
Pathways
• A step frequently encountered in metabolism is
activation
• activation: the formation of a more reactive
substance
• A metabolite is bonded to some other molecule and
the free-energy change for breaking the new bond is
negative.
• Causes next reaction to be exergonic
Two Ways of Looking at Coenzyme A
• Coenzyme A (CoA-SH) contains units of 2-
mercaptoethylamine,
mercaptoethylamine pantothenic acid, and 3’,5’-
ADP
The Hydrolysis of Acetyl-CoA
• The metabolically active form of a carboxylic acid is
the corresponding acyl-CoA thioester, in which the
thioester linkage is a high-energy bond
The Role of Electron Transfer and ATP
Production in metabolism
Summary
• Metabolic pathways proceed in many stages,
allowing for efficient use of energy

• Many coenzymes, particularly coenzyme A(CoA)

play a crucial role in metabolism