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General Biology: Bioenergetics and Enzymes

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  • Bioenergetics

    The study of how energy flows through living organisms, including how cells acquire, transform, store, and use energy.

  • Kinetic energy

    Energy of motion, such as moving molecules, a swimming fish, or flowing electrons.

  • Potential energy

    Stored energy due to an object's location or structure, like water behind a dam or molecules.

  • First Law of Thermodynamics

    Energy can be transferred and transformed but cannot be created or destroyed (conservation of energy).

  • Second Law of Thermodynamics

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

  • Entropy (S)

    A measure of disorder or randomness; higher entropy means more disorder.

  • Spontaneous process

    A process that occurs without outside energy input, increases entropy, and decreases free energy of the system.

  • Free energy (G)

    The portion of a system's energy that can perform work when temperature and pressure are uniform (Gibbs free energy).

  • Equation for change in free energy

    ΔG = ΔH - TΔS, where ΔG is change in free energy, ΔH is change in enthalpy, T is temperature in Kelvin, and ΔS is change in entropy.

  • When is a reaction spontaneous?

    When ΔG is negative (ΔG < 0), meaning free energy decreases and the reaction releases energy.

  • Exergonic reaction

    Releases free energy (ΔG < 0), spontaneous, products have less free energy than reactants.

  • Endergonic reaction

    Absorbs free energy (ΔG > 0), nonspontaneous, products have more free energy than reactants and require energy input.

  • Metabolism

    The totality of an organism's chemical reactions managing material and energy resources.

  • Catabolic reaction

    Breaks down complex molecules into simpler ones, releases energy (exergonic). Example: cellular respiration.

  • Anabolic reaction

    Builds complex molecules from simpler ones, consumes energy (endergonic). Example: photosynthesis.

  • Energy coupling

    Use of an exergonic process to drive an endergonic process.

  • ATP structure

    Adenosine triphosphate: adenine (base) + ribose (sugar) + three phosphate groups.

  • Why are ATP's phosphate bonds called 'high energy'?

    Because the products of hydrolysis (ADP + Pi) are more stable and have lower free energy than ATP, releasing energy.

  • How does ATP hydrolysis drive endergonic reactions?

    Energy released by ATP hydrolysis exceeds energy required by the endergonic reaction, making the overall ΔG negative and spontaneous.

  • Enzyme

    A protein that acts as a biological catalyst, speeding up reactions without being consumed.

  • Activation energy (EA)

    The initial energy needed to start a reaction by contorting reactants so bonds can break.

  • How do enzymes lower activation energy?

    By stabilizing the transition state, lowering the energy barrier so the reaction happens faster without changing ΔG.

  • Active site

    The region of an enzyme where the substrate binds and catalysis occurs, formed by specific amino acids.

  • Induced fit

    The change in shape of the enzyme's active site upon substrate binding, enhancing substrate binding.

  • Competitive inhibitor

    A molecule resembling the substrate that binds the active site, blocking substrate binding; can be overcome by increasing substrate concentration.

  • Noncompetitive inhibitor

    Binds elsewhere on the enzyme, changes its shape, and cannot be overcome by more substrate.

  • Allosteric regulation

    Regulatory molecule binds at a site other than the active site, affecting enzyme activity by stabilizing active or inactive forms.

  • Feedback inhibition

    The end product of a metabolic pathway inhibits an early enzyme in the pathway, preventing overproduction.