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Energy, Metabolism, and Enzyme Function in Cells

스터디 가이드 - 스마트 노트

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Energy and Metabolism

Overview of Metabolism

Metabolism encompasses all chemical reactions within an organism, allowing it to transform matter and energy. These reactions are organized into metabolic pathways, where each step is catalyzed by a specific enzyme.

  • Catabolic pathways: Break down complex molecules into simpler ones, releasing energy (e.g., hydrolysis).

  • Anabolic pathways: Build complex molecules from simpler ones, consuming energy (e.g., dehydration synthesis).

Diagram of a metabolic pathway with sequential enzyme-catalyzed steps

Forms of Energy

Energy exists in various forms and can be converted from one form to another:

  • Kinetic energy: Energy of motion.

  • Thermal energy: Kinetic energy associated with random movement of atoms or molecules.

  • Potential energy: Stored energy due to position or structure.

  • Chemical energy: Potential energy available for release in chemical reactions.

Thermodynamics in Biology

Thermodynamics is the study of energy transformations. Biological systems are open, exchanging energy and matter with their surroundings.

  • First Law of Thermodynamics: Energy cannot be created or destroyed, only transformed or transferred.

  • Second Law of Thermodynamics: Every energy transfer increases the entropy (disorder) of the universe; some energy is lost as heat.

Bear illustrating first and second laws of thermodynamics

Energy Conversion and Entropy

Useful energy is stored in organized matter. When used, some energy is lost as heat, increasing entropy. Living organisms maintain order internally but increase disorder in their surroundings.

Car engine converting chemical energy to kinetic energy and heat

Free Energy and Spontaneity

Gibbs Free Energy (G)

Free energy is the portion of a system's energy that can perform work at constant temperature and pressure. The change in free energy (ΔG) determines whether a process is spontaneous.

  • ΔG < 0: Spontaneous process (releases free energy).

  • ΔG > 0: Nonspontaneous process (requires input of energy).

  • ΔG = G_{final} - G_{initial}

Examples of spontaneous processes: gravitational motion, diffusion, chemical reaction

Exergonic and Endergonic Reactions

  • Exergonic reactions: Release free energy (ΔG < 0), spontaneous.

  • Endergonic reactions: Absorb free energy (ΔG > 0), nonspontaneous.

Graphs comparing exergonic and endergonic reactions

Equilibrium and Metabolism

Cells are open systems and never reach equilibrium, allowing continuous metabolic work. In closed systems, reactions reach equilibrium and stop doing work.

Isolated hydroelectric system reaching equilibrium Open hydroelectric system representing cellular metabolism

ATP: The Energy Currency of the Cell

Structure and Function of ATP

Adenosine triphosphate (ATP) stores and transfers energy for cellular work. It consists of adenine, ribose, and three phosphate groups. Hydrolysis of ATP releases energy by breaking a phosphate bond.

Structure of ATP molecule

The ATP Cycle

ATP is regenerated by adding a phosphate group to adenosine diphosphate (ADP), using energy from catabolic reactions. This cycle couples exergonic and endergonic processes in the cell.

ATP cycle: energy coupling in cells

Enzymes and Metabolic Pathways

Role of Enzymes

Enzymes are biological catalysts that speed up metabolic reactions by lowering the activation energy barrier, without being consumed in the process.

  • Activation energy (EA): The initial energy required to start a reaction.

Activation energy barrier in a chemical reaction Effect of enzyme on activation energy

Enzyme Specificity and Mechanism

Each enzyme acts on a specific substrate, binding at the active site to form an enzyme-substrate complex. The induced fit model describes how the enzyme changes shape to facilitate the reaction.

Enzyme-substrate interaction and induced fit

Factors Affecting Enzyme Activity

  • Temperature: Each enzyme has an optimal temperature for activity.

  • pH: Each enzyme has an optimal pH range.

  • Cofactors: Nonprotein helpers (inorganic ions or organic coenzymes) required for enzyme function.

Enzyme Inhibition

  • Competitive inhibitors: Bind to the active site, blocking substrate binding.

  • Noncompetitive inhibitors: Bind elsewhere, altering enzyme shape and reducing activity.

Competitive and noncompetitive inhibition of enzymes

Allosteric Regulation and Cooperativity

Allosteric enzymes have multiple subunits and can be regulated by activators or inhibitors binding to sites other than the active site. Cooperativity occurs when substrate binding to one active site increases activity at other sites.

Allosteric activation and inhibition of enzymes Cooperativity in allosteric enzymes

Feedback Inhibition

In feedback inhibition, the end product of a metabolic pathway inhibits an enzyme involved early in the pathway, preventing overproduction and conserving resources.

Feedback inhibition in a metabolic pathway

Summary Table: Key Concepts in Energy and Metabolism

Concept

Definition

Example

Catabolic Pathway

Breaks down molecules, releases energy

Cellular respiration

Anabolic Pathway

Builds molecules, consumes energy

Protein synthesis

Exergonic Reaction

Releases free energy (ΔG < 0)

ATP hydrolysis

Endergonic Reaction

Requires energy input (ΔG > 0)

Glucose synthesis

Competitive Inhibition

Inhibitor binds active site

Sulfa drugs inhibiting bacterial enzymes

Noncompetitive Inhibition

Inhibitor binds elsewhere, changes enzyme shape

Heavy metal poisoning

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