Metabolism & Free Energy Flashcards

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1
Q

Metabolism

A

All the chemical reactions occurring in an

organism

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2
Q

Metabolic Pathways

A

a molecule is altered through a series of steps resulting in a specific product
-Catalyzed by enzymes

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3
Q

Catabolic Pathways

A

release energy by breaking down molecules (exergonic)

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4
Q

Anabolic Pathways

A

consume energy to build complicated molecules from simpler ones (endergonic)

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5
Q

Energy

A

the capacity to cause change

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6
Q

Types of Energy

A

kinetic, heat (thermal), potential, chemical

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7
Q

Kinetic Energy

A

energy due to motion

-molecules move due to kinetic energy (ie passive transport)

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8
Q

Heat (thermal) energy

A

affects the speed of molecular movement

-type of kinetic energy

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9
Q

Potential Energy

A

based on position/location in surroundings

-stored energy

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10
Q

Chemical Energy

A

potential energy stored in chemical bonds

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11
Q

1st Law of Thermodynamics

A

Energy of the universe is constant so it can be transferred or transformed but not created or destroyed

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12
Q

2nd Law of Thermodynamics

A

Every energy transformation leads to increased entropy

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13
Q

Free Energy: definition

A

The portion of energy within a system that is free to do work (symbolized by G)

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14
Q

Free Energy: equation

A

ΔG = ΔH – TΔS

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15
Q

If ΔG is a negative value…

A

the process is spontaneous and exergonic & decreases the system’s free energy
– The final state of energy is less likely to change & is
more stable

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16
Q

If ΔG is a positive value…

A

the process requires energy input (endergonic) & increases the system’s free energy

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17
Q

Exergonic Reactions

A
Release energy (ΔG is negative)
– Spontaneous (this doesn’t indicate the required time)
– Ex: Cellular Respiration
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18
Q

Endergonic Reactions

A

Absorbs energy (Δ G is positive)
– Nonspontaneous
– Ex: Photosynthesis

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19
Q

Types of Cellular Work

A

mechanical, transport, chemical

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20
Q

Mechanical Work

A

– Beating cilia
– Contracting muscles
– Moving chromosomes (by spindle fibers during mitosis/meiosis)

21
Q

Transport Work

A

Pumping substances across the cell membrane

and up the concentration gradient

22
Q

Chemical Work

A

– Pushing endergonic reactions

– Creating polymers

23
Q

To manage energy resources, cells use

A

energy coupling

24
Q

Energy Coupling

A

Exergonic processes drive endergonic ones
– ATP is responsible for most coupling in cells and
acts as the immediate power source for work

25
Q

How does ATP release energy?

A

The bonds between the phosphate groups are broken by hydrolysis creating an inorganic phosphate (Pi), ADP, and a release of energy
– The energy released from ATP is greater than most other molecules due to the high negative charge on the phosphate tail

26
Q

ATP & Energy Coupling

A

When ATP is hydrolyzed the free phosphate will be used to phosphorylate other molecules through use of an enzyme
• The phosphorylated molecule is less stable & more reactive & this change allows it to perform work
• This ties together an endergonic reaction with an exergonic one
– Used in cellular work

27
Q

Regeneration of ATP

A

ATP is a renewable resource…just add a phosphate group to ADP
– Requires energy from exergonic reactions in the cell
– Creating and breaking down ATP is known as the ATP Cycle
– performed during cellular respiration

28
Q

Enzyme

A

Catalytic proteins that speed up reactions without being consumed
– Without these many metabolic pathways would
be stuck for years (ex. sucrose hydrolyzed into
fructose and glucose)

29
Q

How do you recognize an enzyme?

A

• It will usually end with –ase
• Conveniently, its name will usually indicated
its substrate

30
Q

Activation Energy

A

Energy input required to start a metabolic process or chemical reaction (EA)
• Determines the rate of reaction
– Many EA are very high & transition states are rarely reached without assistance
– EA is directly proportional to the difficulty of breaking
apart bonds in the substrate

31
Q

Enzyme Action Curves

A

Enzymes lower EA, allowing molecules to absorb enough energy to transition at moderate temperatures & reasonable time frames
• They do NOT change the overall reaction (ΔG)

32
Q

Why isn’t heat used to speed up chemical reactions?

A
  • Heat would increase the rate of all chemical reactions, wasting energy
  • Proteins within cells can be denatured
  • Enzymes are specific, reusable, and energy-efficient
33
Q

Enzymes-Substrate Interaction

A

While the enzyme and substrate are joined the
catalytic action converts the substrate to the
product(s)

34
Q

Enzyme specificity:

A

Each enzyme only catalyzes a specific substrate

35
Q

Active Site

A

the region of the enzyme that binds to the

substrate is the active site

36
Q

Induced fit

A

means active sites are not rigid but change shape slightly once chemical interactions occurs with the substrate to ensure a snug fit
(ie handshake)

37
Q

substrate

A

The molecule an enzyme will act upon

38
Q

How do enzymes lower activation energy?

A
  1. Acting as a template for substrate orientation
  2. Stressing the substrate by bending critical bonds
  3. Providing a favorable mini environment, such as
    a pH pocket
  4. Participating directly in the catalytic reaction by
    providing temporary covalent bonding
39
Q

point of saturation

A

A point of saturation can be reached by
enzymes & the only way to speed up creation
of the product is to create more enzymes

40
Q

temperature

A

– Reaction rates increase with higher temperatures because substrates collide with active sites more frequently (greater kinetic/heat energy)
– Only works to a point because too high of a temperature will cause enzyme denaturation

41
Q

pH

A

There are optimal pH range because too acidic an environment will cause denaturation
– Example: Pepsin works at pH 2 because functions in
our stomach & trypsin works at pH 12 works in the alkaline environment of the small intestine

42
Q

Cofactors

A

Non protein that all function in various ways to increase enzymatic productivity
– Inorganic cofactors examples are Cu, Fe, Zn
– Organic cofactors (coenzymes) such as vitamins

43
Q

Inhibitors

A

Chemicals that selectively inhibit the actions of enzymes
– Are reversible if bond with a weak bond, but can be irreversible if covalently bonded
Many inhibitors are naturally occurring in the cell

44
Q

Competitive Inhibitors

A

Resemble the normal substrate & compete for admission into active site
ex. penicillin

45
Q

Noncompetitive Inhibitors

A

Molecules that bind to a portion of the enzyme away
from the active site (allosteric site)
– Cause the enzyme to change shape & the active site becomes unreceptive
– Ex. DDT

46
Q

Feedback Inhibition:

A

A metabolic pathway is switched off by its end product
• Product inhibits an enzyme in its own pathway by noncompetitive inhibition
– Prevents unnecessary waste from excess products

47
Q

enthalpy

A
total energy (H) or a system
in a spontaneous reaction, enthalpy decreases
48
Q

entropy

A

(S)
the measure of the disorder/randomness of a system
in spontaneous reactions, entropy increases

49
Q

how does ΔG decrease?

A

decrease in enthalpy (H) or increase in entropy (S) and/or temperature