Unit 3: Cellular Energetics (AP BIO)

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Kinetic Energy

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Chapters 8, 9, 10

32 Terms

1

Kinetic Energy

Energy of things in motion

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2

Potential Energy

Energy that things NOT in motion have

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3

Exergonic

Net release of free energy

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4

Endergonic

Absorbs free energy from its surroundings

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5

Free energy

energy available in the system to do the work

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6

Energy Coupling

using the energy released by exergonic reaction to power the uphill motion of endergonic reaction

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7

Enzymes

typically made of proteins, can speed up reactions by holding substrates in optimal position for the

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8

Catabolic

The break down of complex molecules to simpler compounds which results in a net release of energy

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9

Anabolic

Build complicated molecules from simpler ones which results in a net input/consumption of energy

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10

Feedback Inhibition

  • Ex. ATP inhibits catabolism, ADP activates it

The end product of a metabolic pathway influences the continuation of that pathway by interacting with an enzyme that catalyzes an earlier step in the pathway.

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11

First Law of Thermodynamics

Energy cannot be created or destroyed, only transformed. Living systems need to continually acquire and transform energy in order to remain alive.

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12

Second Law of Thermodynamics

Every time energy is transformed there is a loss of usable energy as heat to the surroundings, and the entropy (“disorder”) of the universe increases.

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13

Spontaneity

“energy favorable”

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14

Catalysts

Substances that increase the rate of a chemical reaction by lowering the activation energy of the reaction, without participating in the reaction.

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15

Activation Energy

the initial investment of energy for a starting reaction in order to break bonds.

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16

Co-factors/ co-enzymes

  • organic (co-enzymes: “vitamins”) or inorganic (co-factors: “minerals”)

“Little helpers” that many enzymes require (groups of atoms to be bound to the enzyme.) Involved in allosteric interactions.

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17

Competitive Inhibition

Refers to any substance that occupies the active site of an enzyme that is not the substrate of that enzyme.

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18

Non-Competitive Inhibition or “Allosteric Inhibition”

Affects enzyme structure and function through binding away from the active site (usually changes the shape of the active site).

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19

Allosteric inhibitors

modify the active site of the enzyme so that substrate binding is reduced or prevented.

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20

Allosteric activators

modify the active site of the enzyme so that the affinity for the substrate increases.

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21

Allosteric Regulators

This often happens through cooperativity:

Binding of first substrate increases the affinity for all of the other substrates to bind.

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22

Redox reactions (oxidation-reduction)

atom are oxidized (loss of e-), then reduced (addition of e-)

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23

Electron Shuttles

molecules which can hold electrons when they are taken from molecules and release them to other molecules when needed.

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24

ATP

  • Free energy from metabolism is used to turn a molecule of ADP (2 phosphates) into a molecule of ATP (3 phosphates).

  • The bond between the 2nd and 3rd phosphate is easily broken.

  • The free energy that is released from bonds formed (between water and phosphate) is used to power cellular work.

short-term free energy storage molecule used in all biological systems.

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25

NADH/NAD+ & FAD/FADH2 & NADP+/NADPH

  • Helps with biological energy production by starting redox reactions

Electron shuttles - can hold electrons when they are taken from molecules and release them to other molecules when needed. This transfer of electrons also brings protons along for the ride.

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26

Fermentation

  • Occurs: in the cytoplasm of all anaerobically respiring cells

  • Uses: 2 Pyruvate, 2 NADH

    Produces: A variety of organic molecules depending on the organism, and 2 NAD+

    • Examples of products + 2 NAD+:

      Yeast – ethanol (2 Carbon) and CO2

      Mammalian Muscle Cells – Lactic Acid (3 Carbon)

Fermentation pathways allow cells to oxidize NADH back to NAD+ in order to continue anaerobic cellular respiration. Pyruvate is reduced into one of a variety of molecules.

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27

Glycolysis

Occurs: in the cytoplasm of all cells

Uses: Glucose (6 Carbon), 2 ATP, 2 NAD+

Produces: 2 Pyruvate (3 Carbon), 4 ATP, 2 NADH

1 Glucose is broken into 2 (three carbon) pyruvates.

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28

Pyruvate Oxidation (Link RXN)

1 pyruvate is oxidized (loses e-) to become acetyl CoA, producing one molecule of Co2 (removes one carbon from pyruvate) and 1 NADH

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29

Citric Acid Cycle (Kreb cycle)

Occurs: In the matrix of the mitochondria.

Uses: A molecule of Acetyl-CoA (2 Carbon), 3 NAD+, 1 FAD, and 1 ADP

Produces: 2 CO2, 3 NADH, 1 FADH2, 1 ATP

Note: This happens twice per every 1 glucose.

Stores energy from glucose into electron carriers (NADH and FADH2) to be used in oxidative phosphorylation. Remaining 4 carbons will be released as Co2.

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30

Oxidative Phosphorylation

Occurs: At the inner membrane of the mitochondria

Uses: Oxygen, and all NADH and FADH2 produced in glycolysis (2 NADH), link reaction (2 NADH per glucose), and the citric acid cycle (6 NADH and 2 FADH2 per glucose)

Produces: Water, NAD+, FAD, and >30 ATP

What’s oxidized: NADH and FADH2

What’s produced: ATP and Water

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31

Electron Transport Chain

Electron carriers drop off e-, passes e- across proteins as they are attracted to electronegative o2 at the end of the chain. In the process, H+ ions are sucked through the channel (active transport) because they are attracted to the e- moving through the ETC. The e- are oxidized and reduced until they reach o2 (electron acceptor) which becomes H20.

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32

Chemiosmosis

ATP Synthase (protein channel) takes energy from e- crossing bilayer (passive transport) to turn ADP + Pi (inorganic phosphate) into ATP

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