BackChapter 8: An Introduction to Metabolism – Study Notes
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Metabolism and Thermodynamics in Biology
Overview of Metabolism
Metabolism refers to the totality of an organism’s chemical reactions, encompassing both the breakdown and synthesis of molecules. It is an emergent property of life, arising from the orderly interactions between molecules within cells.
Metabolic Pathways: A series of chemical reactions in which a specific molecule is altered stepwise to produce a product. Each step is catalyzed by a specific enzyme.
Catabolic Pathways: Release energy by breaking down complex molecules into simpler compounds (e.g., cellular respiration).
Anabolic Pathways: Consume energy to build complex molecules from simpler ones (e.g., protein synthesis).
Energy Coupling: Cells manage energy by coupling exergonic (energy-releasing) and endergonic (energy-consuming) reactions.

The Laws of Thermodynamics
Biological processes are governed by the laws of thermodynamics, which describe how energy is transferred and transformed in living systems.
First Law (Conservation of Energy): Energy can be transferred and transformed, but not created or destroyed.
Second Law (Entropy): Every energy transfer increases the entropy (disorder) of the universe. Some energy is lost as heat and becomes unavailable to do work.

Forms of Energy in Biological Systems
Types of Energy
Energy is the capacity to cause change and exists in various forms relevant to biological processes.
Kinetic Energy: Energy associated with motion (e.g., moving water, muscle contraction).
Thermal Energy: Kinetic energy due to random movement of atoms or molecules; transfer is called heat.
Potential Energy: Energy due to location or structure (e.g., water behind a dam, arrangement of electrons in bonds).
Chemical Energy: Potential energy available for release in a chemical reaction (e.g., glucose breakdown).

Free Energy and Spontaneity of Reactions
Free Energy Change (ΔG)
The change in free energy (ΔG) during a reaction determines whether the reaction occurs spontaneously.
Formula: $\Delta G = \Delta H - T \Delta S$ Where: $\Delta G$ = change in free energy $\Delta H$ = change in enthalpy (total energy) $\Delta S$ = change in entropy $T$ = temperature in Kelvin
Spontaneous Reactions: Occur when $\Delta G$ is negative; energetically favorable.
Nonspontaneous Reactions: Occur when $\Delta G$ is zero or positive; require energy input.

Exergonic vs. Endergonic Reactions
Chemical reactions are classified based on their free-energy changes.
Exergonic Reaction: Proceeds with a net release of free energy ($\Delta G < 0$); spontaneous.
Endergonic Reaction: Absorbs free energy from surroundings ($\Delta G > 0$); nonspontaneous.

ATP and Energy Coupling
Structure and Function of ATP
ATP (adenosine triphosphate) is the cell’s primary energy currency, composed of ribose, adenine, and three phosphate groups. It powers cellular work by coupling exergonic and endergonic reactions.
Hydrolysis of ATP: Energy is released when the terminal phosphate bond is broken by hydrolysis.
Phosphorylation: Transfer of a phosphate group from ATP to another molecule, making it more reactive.
ATP Cycle: ATP is regenerated by addition of a phosphate group to ADP, using energy from catabolic reactions.

Cellular Work Powered by ATP
Cells use ATP to perform three main types of work:
Chemical Work: Driving endergonic reactions (e.g., synthesis of macromolecules).
Transport Work: Pumping substances across membranes against concentration gradients.
Mechanical Work: Moving structures within the cell (e.g., muscle contraction, cilia movement).

Enzymes and Metabolic Regulation
Activation Energy and Catalysis
Every chemical reaction requires an initial input of energy, called activation energy (EA), to break bonds in reactants. Enzymes act as catalysts, lowering the activation energy barrier and speeding up reactions without being consumed.
Enzyme Function: Enzymes lower EA, allowing reactions to occur at moderate temperatures.
Enzyme Specificity: Each enzyme is specific to its substrate, binding at the active site.
Induced Fit Model: The enzyme changes shape to fit the substrate, enhancing catalysis.

Factors Affecting Enzyme Activity
Enzyme activity is influenced by environmental conditions and specific chemicals.
Temperature: Each enzyme has an optimal temperature; activity decreases beyond this point due to denaturation.
pH: Each enzyme has an optimal pH, often reflecting its typical environment (e.g., pepsin in stomach, trypsin in intestine).
Cofactors: Nonprotein helpers (inorganic or organic) required for enzyme function. Organic cofactors are called coenzymes (e.g., vitamins).
Inhibitors: Chemicals that reduce enzyme activity. Competitive inhibitors bind to the active site, while noncompetitive inhibitors bind elsewhere, altering enzyme shape.
Factor | Effect on Enzyme Activity |
|---|---|
Temperature | Optimal range increases activity; extreme heat denatures enzyme |
pH | Optimal pH maximizes activity; deviation reduces activity |
Cofactors | Required for proper function; absence reduces activity |
Inhibitors | Competitive: block active site; Noncompetitive: alter enzyme shape |
Summary Table: Exergonic vs. Endergonic Reactions
Type of Reaction | ΔG | Spontaneity | Energy Flow |
|---|---|---|---|
Exergonic | Negative | Spontaneous | Energy released |
Endergonic | Positive | Nonspontaneous | Energy absorbed |
Key Terms and Definitions
Metabolism: All chemical reactions in an organism.
Catabolic Pathway: Breaks down molecules, releases energy.
Anabolic Pathway: Builds molecules, consumes energy.
ATP: Adenosine triphosphate, main energy carrier.
Enzyme: Protein catalyst for biochemical reactions.
Activation Energy (EA): Energy required to start a reaction.
Free Energy (G): Energy available to do work.
ΔG: Change in free energy during a reaction.
Entropy (S): Measure of disorder.
Exergonic Reaction: Releases energy, spontaneous.
Endergonic Reaction: Requires energy, nonspontaneous.
Cofactor: Nonprotein helper for enzyme activity.
Competitive Inhibitor: Blocks active site.
Noncompetitive Inhibitor: Alters enzyme shape.