Chapter 6 - Energy and Life Flashcards

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1
Q

Thermodynamics

A

Study of energy transfer and transformation

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2
Q

Anabolic pathway

A

Build up of simple –> complex molecules

  • dehydration (condensation)
  • endothermic reaction (requires energy input)
    e. g. photosynthesis
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3
Q

Catabolic pathway

A

Breakdown of complex –> simple molecules

  • hydrolysis
  • exothermic reaction (gives out energy)
    e. g. respiration
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4
Q

Energy

A

capacity to cause change

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5
Q

Thermal energy

A

type of kinetic energy

-generated by friction, collision, random movement of particles

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6
Q

Potential energy

A

energy that matter possess as a result of its location, position (gravity, electron shell), structure (chemical energy) and concentration gradient (proton motive force, electrochemical gradient)

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7
Q

Laws of Thermodynamics

A

1) Law of energy conservation
- energy cannot be created/destroyed, only transferred and transformed
2) total entropy of universe must increase
- when energy transfers/transforms, entropy of the universe always increases

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8
Q

Spontaneous reaction

A
occurs without input of energy 
exothermic reactions (ΔG < 0)
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9
Q

enthalpy

A

total energy

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10
Q

Gibbs free energy (G)

A

portion of system’s energy that can do the work
=work capacity
ΔG = ΔH - TΔS

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11
Q

exergonic reaction

A
releases energy (energy of reactants > energy of products)
spontaneous reaction
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12
Q

endergonic reaction

A
requires energy (energy of reactants < energy of products) 
non-spontaneous reaction
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13
Q

Characteristics of unstable systems

A
  • rich in energy (G), highly organized
  • greater work capacity
  • have tendency to change spontaneously to more stable state

will change to decrease the free energy of the system (ΔG < 0), released free energy can be used to do work

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14
Q

Characteristics of stable systems

A
  • lower in energy (G), unorganized

- low working capacity

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15
Q

Energy state in living organisms

A
  • living organisms are open systems that try to move away from equilibrium
  • maintain higher G value - highly organized state and low entropy
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16
Q

ATP

A

Adenosine Triphosphate

-phosphates connected by phosphoanhydride bridge]

17
Q

Spontaneous reaction

A
requires input of energy 
endothermic reactions (ΔG > 0)
18
Q

Non-protein helpers of enzyme activity

A

1) Cofactor
- inorganic transition metals
- prosthetic groups
e. g. Fe, Mg, Cu
2) Coenzyme
- organic
e. g. Vitamin B2 (Riboflavin, FAD+), B3 (Niacin, NAD+) working as electron carriers in cell respiration

19
Q

Prosthetic groups

A
  • type of cofactors
  • emphasizes structural aspect
  • bind tightly to proteins or enzymes —> difficult to remove
20
Q

Lock and Key Model

A

not used

  • unchangeable fitting of complementary shapes (correct size and shape) of the enzyme and its substrate
  • limitation: cannot explain the flexible structure of enzymes
21
Q

Induced Fit Model

A
  • upon substrate binding to enzyme, structural changes occur in active site
  • active site continues to change until the substrate is completely bound to the enzyme’s active site
22
Q

Inhibitor

A

chemicals that inhibit enzyme activity

1) competitive inhibitor
- molecular mimic of substrate
- competes with substrate to bind to active site
- reversible
e. g. molecular mimics like endorphin and morhipne
2) non-competitive inhibitor
- no competition with other substrates
- bind to cell to shape change shape and size
- irreversible

23
Q

Allosteric regulation

A

binding of regulatory molecule to an enzyme’s allosteric site to affect the activity and structure of the enzyme

24
Q

Regulatory molecules

A

1) activator
- promote enzyme activity
e. g. ADP, AMP for cellular respiration
2) inhibitor
- inhibit enzyme activity

25
Q

Cooperativity

A

type of allosteric activation

  • binding of one substrate molecule to active site of one subunit locks all other subunits in active conformation
  • e.g. hemoglobin - active state with allosteric molecule (O2), inactive state without allosteric molecule