Chapter 8 Flashcards

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1
Q

cofactor

A
  • inorganic
  • permanent or temporary
  • sit in active sight to help bonding of enzyme
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2
Q

what is ATP

A
  • fit under nucleic acid category
  • bond between 2nd and 3rd phosphate contribute to ATP being unstable
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3
Q

what makes up ATP

A
  • 3 phosphates
  • base (adenine)
  • sugar (ribose)
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4
Q

phosphorylated

A

phosphate is transferred to a protein
- becomes more reactive and less stable

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5
Q

when is there the most potential energy

A

longest, weakest bonds

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6
Q

when is there the least potential energy

A

shortest, strongest bonds

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7
Q

enthalpy

A
  • potential energy of molecule
  • effect of molecule on surrounding pressure and volume
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8
Q

exothermic reactions

A
  • release heat energy
  • getting energy
  • product have less potential energy than reactants
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9
Q

endothermic reactions

A

-heat energy is taken up
- takes energy
- products have higher potential energy than reactants

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10
Q

entropy

A
  • amount of disorder
  • entropy increases
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11
Q

second law of thermodynamics

A
  • total entropy always increases in a system
  • example: time only moves in 1 direction
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12
Q

Gibbs free energy

A
  • determines whether reaction is spontaneous or requires energy to proceed
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13
Q

spontaneous reaction

A

-release energy (exergonic)
- below 0

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14
Q

nonspontaneous reaction

A
  • requires energy to occur (endergonic)
  • above 0
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15
Q

energetic coupling

A
  • allows chemical energy released from one reaction to drive another reaction
  • one fuels the other
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16
Q

how does energetic coupling work

A
  1. energy is produced
  2. other reactions occur due to the released energy
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17
Q

electron carriers

A

readily donate electrons to other molecules

18
Q

NAD+

A
  • accepts 2 electrons plus one proton to from NADH
  • nicotinamide adenine dinucleotide
  • coenzyme
  • electron carrier
19
Q

FADH2

A

formed by FAD accepting two electrons plus two protons

20
Q

why does ATP provide so much energy

A

due to the structure
- 3 negative charged phosphate groups (lots of potential energy)

21
Q

how does ADP form

A

hydrolysis bond between two outmost phosphate groups

22
Q

what does phosphorylation do to a protein

A

changes its shape

23
Q

what is the goal of enzymes

A
  • help molecules get past tension between each other
  • provide enough kinetic energy to overcome repulsion between electrons
24
Q

where do substrates bind to

A

active site

25
Q

induced fit

A

enzyme changes shape of substrates and bring substrates together to form bonds

26
Q

what bond allows for substrates to bind

A

hydrogen binds

27
Q

transition state

A
  • unstable condition; haven’t fully connected yet
28
Q

activation energy

A

get substrates to finally link together

29
Q

what do reaction rates depend on

A
  • kinetic energy of reactants
  • activation energy of particular reaction
30
Q

when do reactions occur

A

recants have enough kinetic energy to reach transition state

31
Q

what are the 3 enzyme steps

A
  1. initiation- substrates go to active site
  2. transition state facilitation- substrates start to bond and get over activation hump
  3. termination- products made
32
Q

prosthetic groups

A
  • permanently attached to proteins
  • force protein or enzyme to change shape
33
Q

competitive inhibtion

A

molecule competes with substrate for active site

34
Q

allosteric regulation

A

molecule binds at a location other than active site to either activate or deactivate enzyme

35
Q

metabolic pathways

A

series of reactions each catalyzed by a different enzyme
- build biological molecules

36
Q

feedback inhibtion

A

enzyme in pathway is inhibited by final product of pathway
- slow or increase production
- way enzymes are regulated

37
Q

electron donor

A

give electrons

38
Q

electron acceptor

A

accepts electrons

39
Q

energy

A
  • conserved
  • can only be transferred or transformed
40
Q

higher entropy

A

can rearrange while not changing structure (sand pile)

41
Q

lower entropy

A

very few ways to organize without changing shape (sand castle)