Exam 3 Flashcards

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1
Q

Metabolism

A

sum total of all chemical reactions occurring in a biological system at a given time

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2
Q

2 types of metabolism

A

Anabolic reactions - complex molecules made from simple molecules, Energy required
Catabolic reactions - complex molecules broken down to simpler ones, Energy released

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3
Q

Energy

A

capacity to do work, or the capacity for change

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4
Q

Examples of different forms of energy

A

Chemical - stored in bonds
Electrical - separation of charges
Heat - transfer due to temperature difference
Light - electromagnetic radiation stored as protons
Mechanical - energy of motion

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5
Q

Law of thermodynamics

A

apply to all matter and all energy
transformations in the universe, helps us understand how cells harvest and transform energy to sustain life

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6
Q

1st law of thermodynamics

A

Energy is neither created nor destroyed

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7
Q

2nd law of thermodynamics

A

When energy is converted from one form to another, some of that energy becomes unavailable to do work

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8
Q

Potential vs. Kinetic energy

A

Potential - stored energy (stored as chemical bonds, concentration gradient, or charge imbalance)
Kinetic - energy from movement

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9
Q

Entropy

A

(S) measure of disorder in a system it takes energy to impose order on a system, unless energy is applied to the system, it will be randomly arranged or disordered

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10
Q

Enthalpy

A

(H) total energy

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11
Q

Free energy

A

(G) usable energy that can do work

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12
Q

How is change in energy measured

A

Change in energy measured in calories or joules, ΔG = ΔH – TΔS

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13
Q

(-) ΔG

A

free energy is released

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14
Q

(+) ΔG

A

free energy is required

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15
Q

If free energy not available

A

reaction doesn’t occur

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16
Q

Endergonic vs. Exergonic reactions

A

Exergonic reactions: release free energy (‐ΔG), catabolic
Endergonic reactions: consume free energy (+ΔG), anabolic

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17
Q

Why is ATP important?

A

energy transfer in biochemical reactions, important because it acts as the primary energy carrier within living cells, providing readily available energy to power all essential biological processes

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18
Q

Is ATP formation exergonic or endergonic

A

captures and transfers free energy, so an endergonic reaction

19
Q

What about ATP hydrolysis

A

ATP can by hydrolyzed to ADP and Pi, releasing a lot of energy for endergonic reactions

20
Q

ATP hydrolysis reaction equation

A

ATP + H2O ADP + P i + free energy

21
Q

What two characteristics of ATP allow for release of free energy when it’s hydrolyzed

A

Phosphate groups have negative charges and repel each other, and Free energy of the P~O bond is much higher than energy of the O‐H bond that forms after hydrolysis

22
Q

What is meant by “coupling” reactions

A

an energetically favorable reaction (like ATP hydrolysis) is directly linked with an energetically unfavorable (endergonic) reaction

23
Q

Enzymes

A

biological catalysts that act as a framework in which reactions can take place
– Most are proteins

24
Q

What do enzymes do/don’t do

A

they do speed up chemical reactions in the body, making them essential for many processes, including digestion, blood clotting, and growth, they don’t change the overall equilibrium of a chemical reaction, whether the reaction is endergonic or exergonic

25
Q

Activation energy

A

amount of energy required to start a
reaction, can come from heating the system

26
Q

Transition state

A

reactive mode of the substrate (aka – reactant) after there has been sufficient input of energy to initiate the reaction

27
Q

Transition state intermediate

A

unstable reactants with higher free energy

28
Q

Substrates

A

reactants: molecule(s) on which an enzyme exerts its catalytic action

29
Q

Active site

A

place on an enzyme where substrate binds

30
Q

3 mechanisms of enzyme action

A
  • Enzymes can orient substrates so they can react
  • Enzymes can induce strain by stretching substrate, which makes bonds unstable and more reactive to other substrates
  • Enzymes can temporarily add chemical groups
31
Q

2 ways to regulate enzymes

A
  • Regulation of gene expression – how many enzyme molecules are made
  • Regulation of enzyme itself – enzyme shape may change, or enzyme can be blocked by regulators
32
Q

Reversible vs. irreversible inhibition

A

Reversible inhibition: inhibitor bonds noncovalently to the active site, preventing substrate binding
Irreversible inhibition: inhibitor covalently bonds to side chains in active site and permanently inactivates the enzyme

33
Q

Competitive inhibitors

A

compete with natural substrate for binding sites

34
Q

Uncompetitive vs. noncompetitive inhibitors

A

Uncompetitive inhibitors: bind to enzyme‐substrate complex, preventing release of products
Noncompetitive inhibitors: bind to enzyme at site other than the active site

35
Q

Allosteric regulation

A

an effector binds an enzyme at a site different from the active site, changing the enzyme’s shape

36
Q

Commitment step and feedback inhibition

A

Commitment step: first reaction, followed by other reactions in sequence
Feedback inhibition: final product acts as
noncompetitive inhibitor of the first enzyme, shutting down the pathway

37
Q

Do pH and temperature affect enzymes and what happens at high temperatures

A

Yes, it does, higher temperatures cause denaturation in enzymes since most are proteins, causing noncovalent bonds to break and the 2nd and 3rd structures are destroyed

38
Q

5 principles of metabolic pathways

A
  • Complex transformations occur in a series of separate reactions
  • Each reaction is catalyzed by a specific enzyme
  • Many metabolic pathways are similar in all organisms
  • In eukaryotes, metabolic pathways are compartmentalized in specific organelles
  • Key enzymes can be inhibited or activated to alter the rate of the pathway
39
Q

Burning/metabolism of glucose equation

A

C6 H12 O6 + 6 O2 6 CO2 + 6 H2 O + free energy, very exergonic, G= ‐686 kcal/mol, drives endergonic formation of ATP molecules

40
Q

3 catabolic processes that harvest energy from glucose

A
  • Glycolysis (anaerobic)
  • Cellular respiration (aerobic)
  • Fermentation (anaerobic
41
Q

Redox reactions

A

one substance transfers electrons to
another substance, oxidation and reduction always occur together, OIL RIG, when a molecule loses hydrogen atoms (H), it is considered to be oxidized

42
Q

Electron carrier molecules

A

NADH - Nicotinamide Adenine Dinucleotide + H+
FADH2 - Flavin Adenine Dinucleotide + H+
NADPH - Nicotinamide Adenine Dinucleotide Phosphate + H+

43
Q

5 energy yielding metabolic pathways

A

Glycolysis (Either one)
Fermentation (Anaerobic)
Citric Acid Cycle (Aerobic)
Pyruvate Oxidation (Aerobic)
Respiratory chain (Aerobic)