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):

    1. Energy cannot be created or destroyed, only converted from one form to another.

    2. 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

  1. Increase in Volume (e.g., phase change).

  2. Increase in Number (e.g., breakdown of a macromolecule).

  3. Increase in Molecular Random Motion.


Gibbs Free Energy

  • Formula: (ΔG=ΔH−TΔS)(ΔG = ΔH - TΔS)

  • 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 (ΔG=ΔH−TΔS)(ΔG = ΔH - TΔS) 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:
      ATP+H<em>2OightarrowADP+P</em>i+energyATP + H<em>2O ightarrow ADP + P</em>i + energy

    • 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:
      NH<em>3+extGluightarrowextGln+extP</em>i+energyNH<em>3 + ext{Glu} ightarrow ext{Gln} + ext{P}</em>{i} + energy

    • 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.