Metabolism, Energy, and Enzymes

Metabolism: The Chemical Reactions of Life

Food as Fuel and Energy Flow

  • Food Composition: Foods primarily consist of lipids, proteins, and carbohydrates, which are mainly composed of carbon (C), hydrogen (H), and oxygen (O).

  • Oxidation Reaction: Food molecules are oxidized to release energy, following the general reaction: (C, H, O ext{ food molecules}) + O2 ightarrow CO2 + H_2O + ext{energy}.

  • Cellular Chemical Work: All organisms must perform chemical work, including:

    • Energy storage, growth, repair, and replacement of cellular components.

    • Moving molecules and ions across cell membranes.

  • Ecosystem Energy Flow: Energy flows through ecosystems as follows:

    1. Light energy from the sun is captured.

    2. Photosynthesis occurs in chloroplasts, converting $CO2 + H2O$ into organic molecules and $O_2$.

    3. Cellular Respiration takes place in mitochondria, breaking down organic molecules in the presence of $O2$ to produce $CO2 + H_2O + ext{ATP}$.

    4. ATP (adenosine triphosphate) powers most cellular work.

    5. Heat energy is released as a byproduct of these transformations.

Laws of Thermodynamics and Metabolism

  • Metabolism Definition: The totality of an organism's chemical reactions, transforming matter and energy consistent with the laws of thermodynamics.

  • Metabolism Subtypes:

    • Catabolism: Pathways that release energy by breaking down complex molecules into simpler compounds.

      • Example: Proteins, polysaccharides, and fats are broken down into amino acids, monosaccharides, and fatty acids. These further convert to Acetyl CoA, fueling the Citric Acid Cycle and Oxidative Phosphorylation, producing NADH and ATP.

    • Anabolism: Pathways that consume energy to build complex molecules from simpler ones.

      • Example: The synthesis of protein from amino acids.

  • Forms of Energy: Energy is the capacity to cause change and exists in various forms, some capable of performing work.

  • Specific Energy Requirements for Life:

    • Energy must be released gradually from food.

    • Stored in readily accessible forms.

    • Release from storage must be finely controlled, available precisely when and where needed.

    • Just enough heat must be released to maintain a constant body temperature.

    • A form of energy other than heat must be available to drive reactions that are not favorable at body temperature.

  • Reactions in Living Organisms: Follow the same laws and energy requirements as reactions in a chemistry laboratory.

    • Spontaneous Reactions: Favorable in the forward direction, release free energy, which is available to do work.

  • Biological Order and Disorder:

    • Cells create ordered structures from less ordered materials.

    • Organisms replace ordered forms of matter and energy with less ordered forms.

    • Energy flows into an ecosystem as light and exits as heat.

  • First Law of Thermodynamics (Principle of Conservation of Energy):

    • The energy of the universe is constant.

    • Energy can be transferred and transformed, but it cannot be created or destroyed.

  • Second Law of Thermodynamics:

    • Every energy transfer or transformation increases the entropy (disorder) of the universe.

    • During every energy transfer or transformation, some energy is unusable and often lost as heat.

Free-Energy Change (oldsymbol{ ext{ extDelta} G}) and Reaction Spontaneity

  • Determining Spontaneity: To decide if a process is spontaneous, both change in enthalpy ( ext{ extDelta} H) and change in entropy ( ext{ extDelta} S) must be considered.

    • Favorable conditions: ext{ extDelta} H is negative (exothermic) and ext{ extDelta} S is positive (increased disorder) $
      ightarrow$ spontaneous.

    • Unfavorable conditions: Both ext{ extDelta} H positive and ext{ extDelta} S negative $
      ightarrow$ nonspontaneous.

    • Mixed conditions: A process can be unfavorable by enthalpy (positive ext{ extDelta} H) yet be favored by entropy (positive ext{ extDelta} S) and still be spontaneous.

  • **Free-Energy Change ( ext{ extDelta} G) **:

    • A quantity used to account for both ext{ extDelta} H and ext{ extDelta} S when determining spontaneity.

    • Units: kcal/mol or kJ/mol.

    • Formula: ext{ extDelta} G = ext{ extDelta} H - T ext{ extDelta} S where T is the temperature in Kelvins.

    • The value of ext{ extDelta} G determines spontaneity:

      • Exergonic Reactions: Spontaneous reactions or processes that release free energy and have a negative ext{ extDelta} G.

        • Reactants have higher potential energy than products.

        • Example: 6O2 + C6H{12}O6
          ightarrow 6CO2 + 6H2O (combustion of glucose, releases energy).

      • Endergonic Reactions: Nonspontaneous reactions or processes that absorb free energy from their surroundings and have a positive ext{ extDelta} G.

        • Products have higher potential energy than reactants.

        • Example: Glucose + Fructose
          ightarrow Sucrose + H_2O (synthesis of sucrose, requires energy).

  • Activation Energy: The minimum energy needed to start a chemical reaction.

ATP: Adenosine Triphosphate

  • Energy Currency: ATP powers cellular work by coupling exergonic reactions to endergonic reactions.

  • Types of Cellular Work Driven by ATP:

    • Chemical work: Powering synthesis of macromolecules.

    • Transport work: Moving molecules/ions across membranes against their concentration gradient.

    • Mechanical work: Such as muscle contraction or flagellar movement.

  • Energy Coupling: The use of an exergonic process (like ATP hydrolysis) to drive an endergonic one (like synthesis reactions).

  • ATP Hydrolysis: The removal of a phosphate group (PO_3^{2-}) via hydrolysis.

    • Reaction: ATP + H2O ightarrow ADP + HOPO3^{2-} + H^+

    • This is an exergonic reaction, releasing energy: ext{ extDelta} G = -7.3 ext{ kcal/mol}.

    • The energy released is available for cellular work and chemical synthesis.

  • ATP Synthesis (from ADP):

    • Reaction: ADP + HOPO3^{2-} + H^+ ightarrow ATP + H2O

    • This is an endergonic reaction, requiring energy: ext{ extDelta} G = +7.3 ext{ kcal/mol}.

    • Biochemical energy gathered from catabolic (exergonic) reactions is "stored" in ATP.

  • Energy Storage: Energy is primarily stored in the phosphoanhydride bonds of ATP.

  • ATP-ADP Interconversion: This cycle is fundamental for biochemical energy production, transport, and utilization within the cell.

Metabolic Pathways and Energy Production Stages

  • Metabolic Pathways: Sequences of chemical reactions that occur in an organism.

    • Linear pathways: The product of one reaction serves as the starting material for the next.

    • Cyclic pathways: A series of reactions regenerates one of the initial reactants (e.g., Citric Acid Cycle).

    • Spiral pathways: The same set of enzymes progressively builds up or breaks down a molecule.

  • Four Stages of Energy Production (from food):

    1. Digestion: Large food molecules are broken down by digestive enzymes into smaller molecules.

      • Carbohydrates $
        ightarrow$ glucose and other sugars.

      • Proteins $
        ightarrow$ amino acids.

      • Triacylglycerols (fats and oils) $
        ightarrow$ glycerol and fatty acids.

      • These smaller molecules are then transferred to the blood for transport throughout the body.

    2. Acetyl-Coenzyme A Production: Small molecules (from digestion) are further broken down into two-carbon acetyl groups, which attach to Coenzyme A.

      • Structure of Acetyl-CoA: CH_3-C(=O)-S-[Coenzyme ext{ }A]

      • Acetyl-CoA is a crucial intermediate in the breakdown of all classes of food molecules.

      • This stage also produces limited ATP and NADH.

    3. Citric Acid Cycle (Krebs Cycle):

      • Occurs in the mitochondria.

      • Acetyl-group carbon atoms are oxidized to CO_2.

      • Energy is captured in the chemical bonds of reduced coenzymes: NADH and $FADH_2$.

      • Some energy is also stored directly in ATP.

    4. ATP Production (Electron-Transport Chain and Oxidative Phosphorylation):

      • Occurs in the mitochondria.

      • Electrons from the reduced coenzymes (NADH and $FADH_2$) are passed down the electron-transport chain.

      • This process directly produces the majority of the cell's ATP.

      • Finally, electrons combine with hydrogen ions (H^+) from reduced coenzymes and oxygen (O2) to form H2O.

Enzymes: Biological Catalysts

  • Definition: Enzymes are primarily protein catalysts (though some non-protein enzymes, like ribozymes, exist) that significantly speed up biochemical reactions by lowering the required activation energy.

  • Mechanism: Enzymes bind with reactant molecules, called substrates, at their active site, facilitating bond-breaking and bond-forming processes.

  • Specificity: Enzymes are highly specific, typically catalyzing only a single reaction or a small set of very similar reactions.

    • This specificity is determined by the complementary 3D shape of the enzyme and its substrates.

  • Active Site: The specific region on the enzyme where substrate molecules interact.

    • Binding sites: Responsible for binding and orienting the substrate(s).

    • Catalytic site: Reduces the chemical activation energy of the reaction.

  • Induced Fit Model: A mild, dynamic shift in the enzyme's shape occurs at the active site upon substrate binding, optimizing the catalytic efficiency. This is an expansion of the earlier "lock-and-key" model, which proposed rigid complementarity.

  • Protein Structure and Enzyme Function:

    • The 3D shape of an enzyme (a protein) is critically determined by its amino acid sequence.

    • The amino acids within the active site are particularly vital for specific substrate binding and catalytic function.

    • Cellular Environment: Can significantly impact enzyme function:

      • Suboptimal temperatures: Can cause the enzyme to denature (lose its specific 3D shape), leading to loss of function.

      • Suboptimal pHs: Can reduce substrate-enzyme binding and catalytic activity.

  • How Enzymes Lower Activation Energy: Enzymes facilitate reactions by helping substrates reach their transition state through several mechanisms:

    1. Positioning: Orienting two substrates perfectly for reaction.

    2. Optimal Environment: Providing a favorable chemical environment (e.g., acidic or polar) within the active site.

    3. Stress/Contortion: Applying stress to the substrate, making it less stable and more likely to react.

    4. Temporary Reaction: Temporarily reacting with the substrate, chemically changing it into a less stable, more reactive intermediate.

    • After a catalyzed reaction, the product(s) are released, and the enzyme reverts to its original state, ready for another catalytic cycle.

Enzyme Regulation

  • Importance: Regulating enzyme activity allows cells to precisely control their environment and meet specific metabolic needs (e.g., digestive cells working harder after a meal).

  • Regulation Mechanisms:

    • Modifications to environmental factors (temperature, pH).

    • Production of molecules that inhibit or promote enzyme function.

    • Availability of coenzymes or cofactors.

  • Enzyme Inhibition:

    • Competitive Inhibitors: Molecules that have a similar shape to the substrate and compete with the substrate for binding to the active site.

      • They slow reaction rates but do not affect the maximal reaction rate (if substrate concentration is sufficiently high).

    • Noncompetitive Inhibitors: Molecules that bind to the enzyme at a location distinct from the active site (allosteric site).

      • This binding causes a conformational change in the enzyme, resulting in a slower reaction rate and a reduced maximal rate.

    • Maximal Reaction Rate: The speed of a reaction when substrate concentration is not limiting.

  • Allosteric Regulation (a specific type of noncompetitive regulation):

    • Allosteric Inhibitors: Bind to an allosteric site on the enzyme, modifying the active site's shape so that substrate binding is reduced or prevented.

    • Allosteric Activators: Bind to an allosteric site, modifying the active site's shape to increase its affinity for the substrate, thereby enhancing catalysis.

  • Drug Discovery Connection: Pharmaceutical drugs are often developed by identifying and synthesizing inhibitors specific to enzymes involved in disease-related metabolic pathways.

  • Enzyme Cofactors and Coenzymes:

    • Some enzymes require one or more non-protein molecules, called cofactors or coenzymes, to function.

    • Cofactors: Inorganic ions, such as Fe^{++}, Mg^{++}, or Zn^{++}.

      • Example: DNA polymerase requires Zn^{++}.

    • Coenzymes: Organic molecules, including ATP, NADH, and essential vitamins.

      • These molecules are primarily obtained through diet.

  • Feedback Inhibition in Metabolic Pathways:

    • A critical regulatory mechanism where the end product of a metabolic pathway inhibits an upstream step in the same pathway.

    • Example: ATP acts as an allosteric inhibitor for some enzymes involved in cellular respiration, preventing overproduction when energy levels are high.