Sept. 24 - BIOL 1000
Energy and Enzymes Chapter 8
PASS Peer Assisted Study Sessions
Leader: Ruth
Schedule:
Mondays: 3:00 PM - 4:30 PM in Bethune College (BC 202)
Wednesdays: 12:00 PM - 1:30 PM in BC 202
Metabolism
Defined as the chemical reactions of life
Key characteristics:
Require energy
Involve energy transformations
Involve enzymes
Energy
Definition of Energy: The capacity to do work.
Types of Energy:
Potential Energy: Stored energy due to location or structure.
Chemical Potential Energy: Found in chemical bonds.
Kinetic Energy: Energy of motion.
Potential Energy in Chemical Bonds
Potential energy in a covalent bond depends on the position of the shared electrons:
If shared electrons are far from the nuclei of both atoms, the bond has higher potential energy.
Equal sharing of electrons leads to weaker bonds and higher energy.
Unequal sharing results in stronger and lower energy.
Electronegativity values for common elements:
H: 2.2, C: 2.55, N: 3.0, O: 3.44
Kinetic Energy
Definition: Energy of motion.
Conversion: Energy can be converted from one form to another.
Laws of Thermodynamics
Two major laws.
First Law of Thermodynamics (Conservation of Energy):
Energy cannot be created or destroyed, only converted from one form to another.
Energy is conserved and can be transferred or transformed.
Second Law of Thermodynamics:
The total entropy of a system and its surroundings will increase over time.
Energy tends to disperse or spread out if not hindered.
Enthalpy and Entropy
Enthalpy (H): Refers to the total energy in a molecule.
Changes in Enthalpy are denoted as ΔH (in living systems, ΔH approximates changes in potential energy).
Entropy (S): Refers to the amount of disorder.
Energy tends to disperse or spread out, leading to increased entropy.
Examples of Increasing Entropy
Increase in Volume (e.g., phase change).
Increase in Number (e.g., breakdown of a macromolecule).
Increase in Molecular Random Motion.
Gibbs Free Energy
Formula:
Definition of Gibbs Free Energy (G): Portion of a system’s energy available for work.
Changes in free energy are important in chemical reactions in living systems.
Exergonic Reactions:
Characterized by negative ΔG (-ΔG).
Spontaneous and do not require energy input.
Tends to occur when products have lower enthalpy or higher entropy.
Endergonic Reactions:
Characterized by positive ΔG (+ΔG).
Require energy input and are non-spontaneous.
Typically result in products with higher enthalpy and lower entropy.
Chemical Reactions in Living Systems
Combustion of Glucose: Involves changes in both enthalpy and entropy, and is an example of a spontaneous reaction.
Gibbs Free Energy Changes:
The equation is fundamental in understanding metabolic reactions.
Types of Reactions in Metabolism
Catabolic Reactions:
Break down complex molecules into simpler compounds.
Release energy (exergonic).
Example: Starch converts to glucose.
Anabolic Reactions:
Build more complex molecules from simple ones.
Use energy (endergonic).
Example: Protein synthesis from amino acids.
Coupling of Reactions
Endergonic reactions are powered by coupling them with exergonic reactions.
Energy released from catabolic reactions is utilized to power anabolic reactions.
Mechanism of Energy Transfer:
Energy is transferred via phosphate groups or electrons.
Active carrier molecules:
ATP (Adenosine Triphosphate)
FADH2
NADH
ATP (Adenosine Triphosphate)
Function: Stores a large amount of potential energy.
Structure:
Composed of three phosphate groups, ribose, and adenine.
Structural representation: O-P-O-P-O-P-O-CH2
Hydrolysis of ATP:
Process:
Releases approximately -30.5 kJ/mol or -7.3 kcal/mol of energy.
Example of ATP Function: Glutamine Synthesis
Glutamic Acid to Glutamine Reaction:
Reaction:
Positive ΔG for glutamic acid conversion to glutamine: ΔG = +3.4 kcal/mol.
Coupling Reaction:
Attributed to ATP hydrolysis,
Net ΔG: -3.9 kcal/mol makes the pathway exergonic.
Summary of a Coupled Reaction
Energy released from ATP hydrolysis is transferred to substrates by:
Phosphorylation (adding a phosphate group).
This usually causes a change in shape, increasing the free energy and reactivity of the substrate, making it less stable and more reactive.
Key Insight: Exergonic phosphorylation reactions are coupled to endergonic reactions, facilitating metabolic processes.