Chapter 6 Flashcards

(15 cards)

1
Q

Summarize the Second Law of Thermodynamics and include a definition of Entropy (S)

A

Energy transfer or transformation increases a system’s disorder, called entropy.

Entropy: Measure of randomness of molecules in a system

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2
Q

Explain how energy coupling is used to get an endergonic reaction to occur. Which molecule is often broken down to power an endergonic reaction?

A

An endergonic reaction occurs spontaneously if coupled with an exergonic reaction and both energy total change is negative.

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3
Q

Define metabolism and distinguish catabolic and anabolic pathways

A

Metabolism: the sum total of all chemical reactions that occur within an organism

Catabolism: breakdown of molecules

Anabolic: synthesis of molecules

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4
Q

Define equilibrium and explain why most reactions in living systems avoid equilibrium.

A

Equilibrium: a state in which opposing forces or influences are balanced

Cells are open systems, constantly exchanging materials/energy, never staying stable

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5
Q

Explain the statement– Homeostasis and equilibrium are not the same

A
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6
Q

Explain how activation energy determines the rate of the reaction, and give an example of a source of activation energy

A

Activation energy: allows molecules to get close enough causing rearrangement of bonds

Higher activation energy: slower the reaction

Lower activation energy: faster the reaction

Ex: heat

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7
Q

Explain why cold temperatures slow chemical reactions.

A

Molecules move slower and collide less often. Less activation energy

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8
Q

Define the terms catalyst and enzyme. Explain how an enzyme increases the rate of a biochemical reaction, including the effect the enzyme has on activation energy.

A

Catalyst: speeds up the rate of a chemical reaction without changes or consumption by it

Enzyme: proteins

Enzyme speeds up biochemical reactions, lowering activation energy: easier for molecules to react.

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9
Q

Explain why enzymes catalyze one specific chemical reaction

A

Enzymes catalyze one specific reaction because their shape fits only certain molecules.

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10
Q

Explain how substrate concentration and enzyme inhibitors can affect the rate of an enzyme-catalyzed reaction.

A

-Higher substrate concentration speeds up reaction, but too much can slow it

-Inhibitors slow or stop the enzyme by blocking enzyme’s activity

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11
Q

Compare and contrast competitive inhibitors and noncompetitive inhibitors. Connect it to enzyme shape, inhibitor shape and enzyme binding sites (active sites, allosteric sites).

A

Competitive inhibitors:
-block the enzyme’s active site, competing with the substrate.

Noncompetitive inhibitors:
- bind to allosteric site, changing enzyme’s shape and affecting its function in catalyzing

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12
Q

Define Feedback Inhibition

A

When the end product of a reaction slows or stops the enzyme to prevent overproduction.

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13
Q

Summarize two ways that ATP is made in the cell.

A

Substrate level Phosphorylation: An enzyme transfers a phosphate from an organic molecule to ADP to make ATP

Chemiosmosis: Energy stored in an ion electrochemical gradient is used to make ATP from ADP and Pi

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14
Q

Define energy intermediate and identify two examples of energy intermediates used in the cell

A

A molecule that temporarily stores and transfers energy in cells
-ATP
-NADH

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15
Q

Explain how electron movement is related to reduction-oxidation (redox) reactions and relate it to energy transfer.

A

*In redox reactions, electrons are transferred between molecules.

Reduction: addition of electrons from a molecule/atom

Oxidation: removal of electrons from a molecule/atom

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