Lecture 11: Energy, Enzymes, and Metabolism

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Vocabulary practice flashcards covering bioenergetics, thermodynamics, metabolic pathways, free energy calculations, ATP structure and hydrolysis, enzyme catalysis, and enzyme regulation mechanisms.

Last updated 1:38 AM on 9/27/26
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27 Terms

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Bioenergetics

The study of energy flow through a living system or ecosystem.

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Metabolism

The sum of all chemical reactions that take place inside a living organism.

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Metabolic Pathways

A series of interconnected chemical reactions in a cell that convert one or more initial reactants into ultimate products.

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Anabolic Reactions

Metabolic pathways that require an input of energy to synthesize larger, complex molecules from smaller ones.

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Catabolic Reactions

Metabolic pathways that release energy by breaking down large, complex molecules into smaller molecules.

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Kinetic Energy

The type of energy associated with objects or particles in motion.

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Potential Energy

The energy stored in matter due to its position, arrangement, or chemical bonds that has the potential to perform work.

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Gibbs Free Energy (GG)

The amount of usable energy available to perform work in a system during a chemical reaction.

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Gibbs Free Energy Change Equation

The mathematical formula ΔG=ΔH−TΔSΔG = ΔH - T ΔS, where ΔHΔH represents the change in total enthalpy/system energy, TT is absolute temperature in Kelvin, and ΔSΔS is the change in entropy.

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Exergonic Reactions

Spontaneous chemical reactions that release energy, yielding products with less free energy than the reactants (ΔG<0ΔG < 0).

<p>Spontaneous chemical reactions that release energy, yielding products with less free energy than the reactants ($$ΔG < 0$$).</p>
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Endergonic Reactions

Non-spontaneous chemical reactions that require an input of energy, yielding products with more free energy than the reactants (ΔG>0ΔG > 0).

<p>Non-spontaneous chemical reactions that require an input of energy, yielding products with more free energy than the reactants ($$ΔG > 0$$).</p>
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Activation Energy

The initial threshold energy required for a chemical reaction to contort reactant molecules into an unstable transition state so bonds can break or form.

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Transition State

A high-energy, contorted, and highly unstable state of reactant molecules during a chemical reaction that allows bonds to be broken or created.

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First Law of Thermodynamics

The physical law stating that energy cannot be created or destroyed, but can only be transferred or transformed from one form to another.

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Second Law of Thermodynamics

The physical law stating that energy transfers are not completely efficient, resulting in unusable energy lost as heat and an increase in overall system entropy (disorder).

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ATP (Adenosine Triphosphate)

The primary energy currency molecule of cells, consisting of an adenine base, a ribose sugar, and three bound phosphate groups.

<p>The primary energy currency molecule of cells, consisting of an adenine base, a ribose sugar, and three bound phosphate groups.</p>
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Phosphorylation

The chemical transfer of a terminal phosphate group (PO43−PO_4^{3-}) from ATP to another molecule, coupling exergonic energy release to drive endergonic processes.

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ATP Hydrolysis Energy Yields

The exact energy yield released upon cleavage of phosphate groups, where the first and second phosphate groups yield 7.3 kcal/mol7.3\,kcal/mol each, and the third yields 3.4 kcal/mol3.4\,kcal/mol.

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Sodium-Potassium Pump

An active transport integral membrane protein that uses ATP hydrolysis energy to pump 3 Na+3\,Na^+ ions out of the cell and 2 K+2\,K^+ ions into the cell.

<p>An active transport integral membrane protein that uses ATP hydrolysis energy to pump $$3\,Na^+$$ ions out of the cell and $$2\,K^+$$ ions into the cell.</p>
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Catalysts

Substances, such as enzymes, that speed up chemical reaction rates by lowering the activation energy without being consumed by the reaction.

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Induced Fit

A model of enzyme-substrate interaction where a mild conformational shift in the active site shape occurs upon substrate binding to maximize catalytic efficiency.

<p>A model of enzyme-substrate interaction where a mild conformational shift in the active site shape occurs upon substrate binding to maximize catalytic efficiency.</p>
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Competitive Inhibitors

Inhibitor molecules that structurally resemble the substrate and directly compete for binding at the active site of an enzyme.

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Noncompetitive Inhibitors

Inhibitors that bind to an enzyme at a site other than the active site, slowing down the overall reaction rate by altering enzyme function.

<p>Inhibitors that bind to an enzyme at a site other than the active site, slowing down the overall reaction rate by altering enzyme function.</p>
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Allosteric Regulation

Enzyme regulation where allosteric inhibitors modify the active site to decrease substrate binding, while allosteric activators modify the active site to increase substrate affinity.

<p>Enzyme regulation where allosteric inhibitors modify the active site to decrease substrate binding, while allosteric activators modify the active site to increase substrate affinity.</p>
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Cofactors

Inorganic ions, such as Fe2+Fe^{2+}, Mg2+Mg^{2+}, or Zn2+Zn^{2+} (e.g., Zn2+Zn^{2+} required by DNA polymerase), that are necessary for proper enzyme function.

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Coenzymes

Non-protein organic helper molecules, such as ATP, NADH+NADH^+, and dietary vitamins, required to assist enzyme activity.

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Feedback Inhibition

A metabolic pathway control mechanism where the final end product binds to and inhibits an enzyme operating at an earlier step in the pathway.

<p>A metabolic pathway control mechanism where the final end product binds to and inhibits an enzyme operating at an earlier step in the pathway.</p>