Chapter 6 Bio 201
Chapter 6: Energy and Metabolism
Introduction to Energy and Metabolism
Energy as a Fundamental Requirement for Life
Life is defined by properties that require energy.
Energy flow is essential for the functioning of living organisms.
Thermodynamics and Energy Flow
Thermodynamics
Study of energy changes in chemical systems.
Organisms obey the laws of physics and chemistry.
Types of Energy
Definition of Energy
Capacity to do work.
Two main states:
Kinetic Energy: Energy of motion.
Potential Energy: Stored energy that can enable motion.
Forms of energy include mechanical, heat, sound, electric, light, and radioactivity.
Measurement of Energy
Units of Energy
Heat: Convenient measure of energy.
Biological Unit: Kilocalorie (kcal).
1 kcal = heat required to raise 1 kg of water by 1°C.
The calorie with a capital C on food labels refers to 1 kcal.
Physics Unit: Joule (J).
1 J = 0.239 cal.
Energy in Biological Systems
Energy Capture
Energy flows from the sun into the biological world.
Photosynthetic organisms capture this energy, storing it in chemical bonds of molecules like sugars.
Breaking chemical bonds requires energy, which can then be used to form new bonds.
Redox Reactions
Oxidation and Reduction
Oxidation: Loss of an electron; occurs frequently with oxygen as the electron acceptor.
Reduction: Gain of an electron.
These processes are always paired in oxidation-reduction reactions (redox).
Laws of Thermodynamics
First Law of Thermodynamics
Energy is conserved; it cannot be created or destroyed.
Energy can change forms (e.g., from potential to kinetic).
Total energy in the universe remains constant, but some is lost as heat during transformations.
Second Law of Thermodynamics
Entropy (disorder) of the universe is increasing.
Energy transformations are never 100% efficient; some energy becomes unavailable.
Systems move toward less ordered states spontaneously.
Free Energy (Gibbs Free Energy)
Definition
Free energy (G) is the energy available to perform work.
Formula: G = H − TS
H = enthalpy (total energy), T = absolute temperature, S = entropy.
Change in Free Energy (ΔG)
Positive ΔG indicates non-spontaneous reactions (endergonic), requiring energy input.
Negative ΔG indicates spontaneous reactions (exergonic), releasing energy.
Energy in Chemical Reactions
Activation Energy
Extra energy is needed to destabilize bonds and initiate a chemical reaction.
The rate of reaction is influenced by the activation energy needed.
Reaction rates can be increased by raising the energy of reactants or lowering the activation energy using catalysts.
Catalysts in Biological Reactions
Function of Catalysts
Catalysts lower the activation energy required for reactions.
Enzymes are biological catalysts that increase the rate of reactions without being consumed.
Adenosine Triphosphate (ATP)
Structure and Function
ATP is the primary energy currency in cells, composed of ribose, adenine, and a chain of three phosphates.
Energy is released upon hydrolysis of ATP to ADP and Pi (inorganic phosphate).
ATP hydrolysis drives endergonic reactions in the cell but is not suitable for long-term energy storage; fats and carbohydrates are preferred.
Enzyme Activity and Regulation
Basic Characteristics of Enzymes
Enzymes bind substrates at their active sites to form enzyme-substrate complexes, facilitating reactions via induced fit.
Enzymes can be influenced by environmental factors such as temperature and pH, and their activity may be altered by inhibitors or activators.
Inhibition Mechanisms
Types of Inhibition
Competitive Inhibitors: Compete with substrate for the active site.
Noncompetitive Inhibitors: Bind to the enzyme elsewhere, affecting activity without competing with the substrate.
Allosteric Regulation: Enzymes can exist in active or inactive forms, with allosteric sites affecting their function.
Feedback Inhibition
Mechanism of Feedback Inhibition
End products of a biochemical pathway may inhibit earlier steps, preventing waste of resources and energy.
This regulatory mechanism ensures metabolic efficiency and balance in the cell.