Chapter 6: Energy and Metabolism Flashcards

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Comprehensive vocabulary flashcards covering basic thermodynamics, free energy equations, enzyme structure/function, activation energy, ATP dynamics, and metabolic regulation from Chapter 6.

Last updated 5:07 PM on 10/6/26
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36 Terms

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Energy

The capacity to do work, which exists in potential and kinetic states.

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<p>Potential Energy</p>

Potential Energy

Stored energy, such as chemical energy stored in the covalent bonds of molecules.

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<p>Kinetic Energy</p>

Kinetic Energy

The energy of motion.

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Heat

A measure of the random movement of molecules; the most convenient form of energy to measure.

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Kilocalorie (kcal)

A unit equal to 1000 calories1000\text{ calories} (or 1 Calorie1\text{ Calorie} on food labels), where 1 calorie1\text{ calorie} is the heat needed to raise 1 g1\,g of water by 1∘C1^\circ\text{C}.

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Oxidation

A chemical reaction in which an atom or molecule loses an electron.

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Reduction

A chemical reaction in which an atom or molecule gains an electron.

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Redox Reactions

Paired oxidation-reduction reactions key to energy flow in biological systems, where an electron lost by one atom is picked up by another.

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First Law of Thermodynamics

The principle that energy cannot be created or destroyed, but can only change from one form to another.

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Second Law of Thermodynamics

The principle stating that energy conversions are not completely efficient and that energy is lost as disorder increases.

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Entropy

The amount of disorder in a system.

<p>The amount of disorder in a system.</p>
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Free Energy

The energy available to break and reform chemical bonds and do work in a system, expressed as ΔG=ΔH−TΔS\Delta G = \Delta H - T\Delta S.

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Enthalpy (H)

The energy contained in the chemical bonds of a molecule or system.

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Endergonic Reaction

A nonspontaneous reaction requiring an input of energy, in which the products contain more free energy than the reactants (ΔG>0\Delta G > 0).

<p>A nonspontaneous reaction requiring an input of energy, in which the products contain more free energy than the reactants ($$\Delta G > 0$$).</p>
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Exergonic Reaction

A spontaneous reaction that releases free energy, in which the products contain less free energy than the reactants (ΔG<0\Delta G < 0).

<p>A spontaneous reaction that releases free energy, in which the products contain less free energy than the reactants ($$\Delta G < 0$$).</p>
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Activation Energy

The extra energy required to destabilize existing chemical bonds and initiate a chemical reaction.

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Catalysis

The process of stressing chemical bonds to lower activation energy, accelerating both forward and reverse reactions without altering the change in free energy.

<p>The process of stressing chemical bonds to lower activation energy, accelerating both forward and reverse reactions without altering the change in free energy.</p>
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Adenosine Triphosphate (ATP)

A nucleotide composed of ribose, adenine, and three strongly repulsive phosphate groups that acts as the cell's energy currency.

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ATP-ADP Cycle

The cyclical system in which ATP is synthesized from ADP and PiP_i using exergonic energy, and hydrolyzed to provide energy for endergonic cellular processes.

<p>The cyclical system in which ATP is synthesized from ADP and $$P_i$$ using exergonic energy, and hydrolyzed to provide energy for endergonic cellular processes.</p>
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Substrate

A specific reactant molecule that binds to an enzyme to undergo a chemical reaction.

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Active Site

A cleft or pocket on the surface of an enzyme where substrate binding and catalysis take place.

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Enzyme-Substrate Complex

The complex formed when a substrate molecule binds to the active site of an enzyme.

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<p>Induced Fit</p>

Induced Fit

The slight conformational change in an enzyme caused by substrate binding that facilitates catalysis or the binding of additional substrates.

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Multienzyme Complex

An assembly of several enzymes that catalyze sequential steps in a metabolic pathway.

<p>An assembly of several enzymes that catalyze sequential steps in a metabolic pathway.</p>
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Ribozymes

Nonprotein RNA molecules capable of intramolecular or intermolecular catalysis.

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Optimum Temperature

The temperature at which an enzyme functions most efficiently, corresponding to 35–40∘C35\text{--}40^\circ\text{C} for most human enzymes.

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Optimum pH

The pH range at which ionic interactions maintain optimal enzyme structure and activity, typically pH 6–86\text{--}8 for most human enzymes.

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Competitive Inhibitors

Regulatory molecules that decrease enzyme activity by competing directly with the substrate for binding at the active site.

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<p>Allosteric Site</p>

Allosteric Site

A specific regulatory site on an enzyme distinct from the active site, serving as a chemical on/off switch when bound by inhibitors or activators.

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Cofactors

Additional nonprotein chemical components, such as inorganic metal ions (zinc, molybdenum, manganese), that assist enzyme function.

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Coenzymes

Nonprotein organic cofactor molecules, such as vitamins B6 and B12, that aid enzyme function.

<p>Nonprotein organic cofactor molecules, such as vitamins B6 and B12, that aid enzyme function.</p>
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Metabolism

The sum total of all chemical reactions carried out by an organism.

<p>The sum total of all chemical reactions carried out by an organism.</p>
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Anabolism

Metabolic reactions that expend energy to build complex molecules from simpler ones.

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Catabolism

Metabolic reactions that harvest energy by breaking down complex molecules.

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Biochemical Pathways

Sequential enzymatic reactions serving as organizational units of metabolism, where the product of one step becomes the substrate for the next.

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Feedback Inhibition

A control mechanism in which the final end-product of a pathway binds to the allosteric site of the first enzyme, inhibiting the pathway when the product is abundant.

<p>A control mechanism in which the final end-product of a pathway binds to the allosteric site of the first enzyme, inhibiting the pathway when the product is abundant.</p>