Chapter 6 Flashcards

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1
Q

Metabolism

A

All chemical rxns in cell (catabolic and anabolic)

Bioenergetics, energy flow, through a living system

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2
Q

Catabolic

A

break down/degradation
release energy

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3
Q

Anabolic

A

Biosynthesis
absorb energy

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4
Q

carbohydrate metabolism

A

cellular respiration (catabolic) in animal cells
photosynthesis (anabolic) in plant cells

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5
Q

Cellular respiration

A

catabolic, breakdown sugar
C6H12O6 + 6O2 -> 6CO2 + 6H2O + energy

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6
Q

Photosynthesis

A

anabolic, synthesize sugar
6CO2 + 6H2O + energy -> C6H12O6 + 6O2

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7
Q

energy

A

ability to do work, bring about change
joules or calories

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8
Q

Important types of energy

A

Solar (photons)
Chemical (chemical bonds)
mechanical (muscular contraction, cellular movement)

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9
Q

Potential energy

A

Stored energy

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10
Q

Kinetic energy

A

Energy of motion

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11
Q

“free” energy

A

Gibbs free energy Willard Gibbs (1878)
portion of system energy available to preform work at uniform (temp/pressure)

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12
Q

change in G = change in H - (T x change in S)

A

H = enthalpy ( total energy )
S = entropy (disorder)
T = absolute temp (kelvin)

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13
Q

negative change in G

A

spontaneous process
change in H negative
Tchange in S very positive

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14
Q

change in G

A

G final - G initial
more to less free energy
system becomes more stable and energy released can be used

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15
Q

exergonic reactions

A

“energy outward”
net release
change in G = negative
spontaneous, released E to surroundings
metabolism -> heat
more reactants than products
high to low GFE

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16
Q

Endergonic reactions

A

“energy inward”
net input
change in G = positive
not spontaneous
requires E from surroundings
coupled with exergonic rxn.s
low to high GFE

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17
Q

Metabolism equilibrium

A

never at equilibrium

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18
Q

activation energy

A

energy required to start reaction
High AE -> slows rxn
Low AW -> quickens rxn

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19
Q

Energy and reactions

A

“contorts” reactants
transition state
allows rxn. to occur

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20
Q

Thermodynamics

A

Study of energy flow/transfer of physical matter
in a system/environment

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21
Q

1st law of conservation of energy

A

Energy cannot be created or destroyed, can be transferred/transformed, and can go from one form to another

22
Q

Thermodynamics does not

A

Indicate if process is possible, will occur spontaneously, or what conditions are needed for the process

23
Q

2nd law of thermodynamics

A

Energy transformations loose useable energy
Every transformation makes the universe less organized/ less organized, more disordered

24
Q

Entropy

A

disorder

25
Q

Universe prefers

A

entropy/disorder
less energy to be disordered

26
Q

Relative disorganization

A

S; disorder; at the end of process there’s less energy and more S

27
Q

ATP structure

A

Nucleotide (adenine)
5 carbon sugar (ribose)
= adenosine
3 phosphates (triphosphate

28
Q

ATP function

A

Chemical (anabolism)
Transport (protein pumps)
Mechanical (cilia movement)

29
Q

Coupled reactions

A

exergonic energy fuels endergonic rxns

30
Q

Adenosine triphosphate

A

ATP
energy currency of cells
Hydrolysis rxn -> water cuts P off
Uses ATP to create ADP P and energy
converts to ADP and creates energy

31
Q

Adenosine diphosphate

A

ADP
Dehydration rxn. -> produce H2O
glucose degradation
uses energy ADP and P to make ATP

32
Q

Coupled reactions

A

one reaction endergonic one exergonic
exergonic (ATP) fuels process
phosphorylation (phosphate transfer) (ADP + P = ATP)

33
Q

Enzymes

A

Catalyze metabolic rxns
most require energy input
lower activation energy
enzyme doesnt change
get energy out dont produce energy
makes rxn. more likely to occur

34
Q

-ase

A

enzymes

35
Q

Lock-n-key model

A

substrate acts as key to specific enzyme
interact via H bonds or ionic bonds
initially thought

36
Q

Induced fit model

A

Binding causes confirmation change
interactions close together
enhance catalytic ability

37
Q

active sites

A

lower activation energy
template for multiple substrates to combine
R group microenvironment
distort substrate shape and increase reactivity
direct temporary chemical interactions

38
Q

rate of enzymatic catalysis

A

Increased concentration of substrate increases rate of reaction to a point
then reaction rates decline and must add more enzyme
temp, pH, cofactors, coenzymes effect

39
Q

Anabolic reaction

A

synthesis reaction enzymatic

40
Q

Catabolic reaction

A

Degradation reaction enzymatic

41
Q

Native function and activity

A

Native shape
effected by change in concentration of substrate, optimal conditions, cofactors, coenzymes

42
Q

cofactors

A

inorganic ions required for enzymes role

43
Q

coenzymes

A

organic molecules, help enzymes function by combining with them

44
Q

Inhibitors

A

Prevent enzyme from operating
competitive and noncompetitive

45
Q

Competitive inhibitors

A

bind to active site and prevent substrate from binding

46
Q

Noncompetitive inhibitors

A

bind to another site on enzyme which causes the enzyme to change shape so substrate cannot bind

47
Q

Allosteric activation/inhibition

A

process when noncompetitive inhibitor bonds to enzyme at secondary site changing function

48
Q

Activator in allosteric activation

A

stabilizes function form

49
Q

Inhibitor in allosteric activation

A

stabilizes inactive form

50
Q

Cooperativity in allosteric activation

A

binding on one side increases likelihood for bonding on another
multi-site enzyme/protein

51
Q

Feedback inhibition

A

Reaction halted by product produced by reaction
binds to enzyme
ATP pathways; help save glucose