Energy and Enzymes Flashcards

(54 cards)

1
Q

How do you know if a reaction has positive or negative enthalpy?

A
  • exothermic: negative because products have less potential energy than reactants)
  • endothermic: positive because heat is taken up
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2
Q

What is enthalpy and what is its letter?

A
  • total energy in a molecule
  • H
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3
Q

What are the characteristics of enthalpy?

A
  1. potential energy of the molecule
  2. effect of the molecule on surrounding pressure and volume
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4
Q

What is entropy and what is its letter?

A
  • amount of disorder OR energy distribution/dispersal
  • S
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5
Q

If entropy is positive…

A

products are less ordered than reactants

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6
Q

If entropy is negative…

A

products are more ordered than reactants

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7
Q

What is Gibbs Free Energy and what is its letter?

A
  • total energy in a rxn available to do work
  • G
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8
Q

If delta G is negative, the reaction is…

A

exergonic and spontaneous

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9
Q

If delta G is positive, the reaction is…

A

endergonic and nonspontaneous

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10
Q

If delta G = 0, the reaction is…

A

at equilibrium

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11
Q

Gibbs Free Energy does not require….

A

the addition of external energy

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12
Q

How do we determine delta G?

A

delta G = delta H - T x delta S

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13
Q

As temperature increases…

A

rate and concentration also increase

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14
Q

Nonspontaneous rxns are driven using…

A

chemical energy

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15
Q

What is energetic coupling?

A

free energy released from an exergonic rxn drives an endergonic rxn

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16
Q

What are the two ways energetic coupling occurs?

A
  1. transfer of electrons
  2. transfer of a phosphate group
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17
Q

What is OIL RIG?

A
  • Oxidation Is Loss
  • Reduction Is Gain
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18
Q

O2 is almost always the ______ agent EXCEPT with _______.

A

oxidizing
fluorine

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19
Q

ATP transfers energy via ___________.

A

phosphate groups

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20
Q

Energy is _________ when ATP is __________.

A

released; hydrolyzed

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21
Q

Energy coupling uses _______ to rip off ____________.

A

ATP; phosphate groups

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22
Q

On a graph, an endergonic rxn starts….

23
Q

On a graph, an exergonic rxn starts…

24
Q

What is a transition state?

A

intermediate point between breaking old bonds and forming new bonds (very unstable w/ very high energy)

25
What is activation energy?
minimum energy required to form the transition state
26
Enzymes are biological ________.
catalysts
27
What is a catalyst?
speeds up a chemical rxn without being used up or changed in the process
28
Reactants are also known as _______.
substrates
29
Substrates bind a react in an __________.
active site
30
What are the steps of an enzyme catalyzed rxn?
1. initiation: enzymes bring substrates together in a precise orientation 2. transition state facilitation: enzymes lower Ea by stabilizing transition state 3. termination: products have a low affinity for the active site and are released
31
How do active sites hold substrates in precise orientation?
hydrogen bonds or other weak interactions
32
What is induced fit?
upon binding substrates, enzymes change conformation (shape)
33
Enzymes are able to stabilize...
transition states
34
What do enzymes NOT change?
delta G and the energies of the reactants/products
35
Enzymes can also work with...?
cofactors, coenzymes, and prosthetic groups
36
What are cofactors?
metal ions (Zn2+, Mg 2+, Fe 2+)
37
What are coenzymes?
organic molecules (NAD+, FAD, coenzyme-A)
38
What are prosthetic groups?
atoms or molecules that are permanently attached to proteins
39
What are some examples of prosthetic groups?
1. heme groups (hemoglobin- carry oxygen) 2. Retinal (vitamin A-basis of vision)
40
At extreme conditions, what happens to enzymes?
denaturation
41
What determines an enzyme's optimal temp and pH?
location (environment helps optimize)
42
Why does a curve eventually reach a plateau?
the enzymes run out/max out
43
How can you increase the max speed of a rxn?
increase amount of enzymes
44
How are enzymes regulated?
covalent modification (long-term)
45
What is covalent modification?
1. cleavage of peptide bonds: can convert enzyme into its functional form (proenzyme) 2. addition of a phosphate group: enzyme changes shape, which changes function
46
How are enzymes regulated (reversible)?
noncovalent interactions
47
What are noncovalent interaction?
1. competitive inhibition 2. allosteric inhibition (noncompetitive) 3. allosteric activation
48
What is competitive inhibition?
- other molecules compete for active site w/ substrate
49
What is allosteric inhibition?
- "different structure" - inhibitor binds to a different site on the enzyme
50
What is allosteric activation?
makes active site more accessible to substrate
51
What are catabolic pathways?
break down molecules, typically releasing energy (ex cellular respiration)
52
What are anabolic pathways?
synthesize molecules, typically requiring energy (ex photosynthesis)
53
How are metabolic pathways inhibited?
feedback inhibition
54
What is feedback inhibition?
- product of a metabolic pathway inhibits an enzyme earlier in the pathway - acts in reverse - prevents the enzyme from starting