Ch 6 Flashcards

1
Q

Q: What is the first law of thermodynamics?

A

A: Energy cannot be created or destroyed; it can only change form. The total amount of energy in the universe is constant.

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2
Q

Q: What is entropy, and how does it relate to systems?

A

A: Entropy is the measure of disorder. As systems lose energy, they become more disorganized, and they naturally move toward maximum entropy.

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3
Q

Q: What is the second law of thermodynamics?

A

A: Energy spontaneously flows from high- to low-quality forms, increasing disorder (entropy).

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4
Q

Q: How does life maintain organization despite entropy?

A

A: Life uses energy from the sun to maintain a high degree of organization.

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5
Q

Q: What are reactants and products in a chemical reaction?

A

A: Reactants are the starting substances in a reaction, while products are the substances formed as a result of the reaction.

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6
Q

Q: What is the difference between endergonic and exergonic reactions?

A

A: Endergonic reactions require energy input (e.g., photosynthesis), while exergonic reactions release energy (e.g., aerobic respiration).

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7
Q

Q: What is activation energy?

A

A: Minimum amount of energy required to start a reaction.

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8
Q

Q: How does ATP act as the cell’s energy currency?

A

A: ATP stores energy by linking a phosphate to ADP (phosphorylation) and releases it by donating a phosphate group to other molecules.

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9
Q

Q: What are cofactors, and what do they do?

A

A: Cofactors, including metal ions and coenzymes, help enzymes by transferring electrons, atoms, or functional groups.

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10
Q

Q: How do transport proteins influence reactions?

A

A: Transport proteins move solutes across membranes, altering their concentration and affecting reaction rates.

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11
Q

Q: How do enzymes speed up reactions?

A

A: Enzymes act as catalysts, lowering the activation energy required for reactions to proceed.

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12
Q

Q: What is the transition state in a reaction?

A

A: The transition state occurs when reactants have absorbed enough energy to overcome activation energy and proceed spontaneously.

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13
Q

Q: What is the induced-fit model of enzyme activity?

A

A: The induced-fit model describes how enzymes adjust their shape slightly to better bind the substrate and catalyze the reaction.

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14
Q

Q: How do temperature, pH, and salinity affect enzymes?

A

A: Extreme conditions can denature enzymes by disrupting their shape, and reduces their function.

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15
Q

Q: What are antioxidants, and how do they assist enzymes?

A

A: Antioxidants like Vitamin E and catalase neutralize free radicals, protecting enzymes and other molecules from damage.

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16
Q

Q: What are metabolic pathways, and what are their types?

A

A: Sequences of enzyme-mediated reactions. They can be linear, cyclic, or branched.

17
Q

Q: What is feedback inhibition?

A

A: Occurs when the end product of a metabolic pathway inhibits an earlier step, preventing overproduction.

18
Q

Q: What are allosteric enzymes?

A

A: Allosteric enzymes have regulatory sites where molecules can bind to inhibit or activate the enzyme’s function.

19
Q

Q: How can chemical reactions reverse direction?

A

A: If products accumulate beyond what the system needs.

20
Q

Q: What is bioluminescence, and how does it occur?

A

A: Light production by organisms, powered by ATP and oxygen reacting with luciferin via luciferase enzymes.

21
Q

Q: How is bioluminescence used in research?

A

A: Biologists use bioluminescent genes to detect bacterial infections and track cellular activity in biofilms.