(Dr. McLachlin) (Unit B) Topic Note 8 Flashcards

1
Q

What is required to determine if a chemical reaction requires energy to procedd in a particular direction?

A

Change in Gibbs free energy
* ΔG = Gproducts - Greactants

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2
Q

When is ΔG negative?

A

When G of reactants is higher than G of the products
* Reaction is spontaneous and energetically favorable

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3
Q

Le Chatelier’s Principle

A

Reaction shifts to counteract any change that is made
* Happens to reactions at equilibrium, when reactions are reversible

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4
Q

How do energetically unfavorable processes occur?

A
  1. Reaction coupling: Couple the reaction to an energetically unfavorable one so that the total net ΔG is negative
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5
Q

What kind of bond does ATP have?

A

“High-energy” phosphoanhydride bond

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6
Q

What can ATP be hydrolyzed into?

A
  • ADP + Pi
  • AMP + PPi (pyrophosphate)
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7
Q

Metabolism

A

The combined sum of the chemical reactions that occur in living organisms

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8
Q

What is metabolism split into?

A
  • Catabolism: Breaking down of large molecules into smaller ones
  • Anabolism: Combining of small molecules to make larger ones
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9
Q

What reactions of optimal points to control the flux through a metabolic pathway?

A

Irreversible reactions
* They are far away from the equilibrium

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10
Q

What would increasing the activity of an enzyme catalyzing a reversible reaction result in?

A

Increased rate of reaction in both directions, with little/no net effect

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11
Q

What are two important mechanisms used to rapidly change enzyme activity?

A
  1. Allosteric regulation
  2. Covalent modification
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12
Q

Allosteric enzymes can bind…

A

Effectors
* At sites other than the active site

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13
Q

What does binding of effectors cause?

A

Conformational changes in the enzyme that increase of decrease its activity

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14
Q

What function does PEP have on phosphofructokinase?

A

Effector, feedback inhibition
* Meatbolite in a metabolic pathway inhibits an enzyme that function earlier in the pathway

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15
Q

Does allosteric inhibition obey Michaelis-Menten kinetics?

A

No it does not

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16
Q

What is one group that commonly regulates enzyme activity?

A

Phosphate

17
Q

What is the phosphorylation state of a target enzyme controlled by?

A
  • Protein kinase: Adds phosphate
  • Protein phosphatase: Removes phosphate
18
Q

What is phosphorylation used for?

A

Used to transmit and amplify signals from outside the cell to the nucleus to control gene expression

19
Q

Reduction vs. Oxidation

A
  • Reduction: Gain of electrons
  • Oxidation: Loses electrons
20
Q

What are two key biological molecules involved in red-ox reactions?

A
  • Nicotinamide Adenine Dinucleotide (NAD)
  • Nicotinamide Adenine Dinucleotide Phosphate (NADP)
21
Q

What are the oxidized forms of NAD and NADP?

A
  • NAD+
  • NADP+
22
Q

What are the reduced forms of NAD and NADP?

A

Add a H- ion
* NADH
* NADPH

23
Q

What is the reducing power of NADH used for?

A

Regenerate ATP from ADP

24
Q

What is the reducing power of NADPH used for?

A

Used in the synthesis of biomolecules, notably fatty acids and cholesterol

25
Q

Describe:

Ubiquinone

A

Also known as Coenzyme Q or simply, Q
* Has a long hydrophobic polyisoprene tail
* Can accept electrons temporarily

26
Q

What is the reduced form of ubiquinone?

A

QH2

27
Q

NADH vs. QH2

A
  • Both are used to generate ATP
  • NADH is water soluble
  • QH2 is very hydrophobic
28
Q

Where are QH2 molecules found?

A

Embedded in the inner mitochondrial membrane