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Ap Biology > energy > Flashcards

energy Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

thermal energy

A

chemical energy stored in bonds of molecules and kinetic energy of brownian motion

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2
Q

temperature

A

average kinetic energy of molecules

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3
Q

heat

A

flow of kinetic energy from one object/ place to another

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4
Q

metabolic pathways

A

a series of chemical reactions resulting in a set product, each catalyzed by different enzymes

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5
Q

catabolism

A

energy releasing pathways (degradative)

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6
Q

Anabolism

A

pathways that consume energy to build complex molecules (biosynthetic)

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7
Q

first law of thermodynamics

A

conservation of energy, energy cant be created or destroyed, only converted from one form to another

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8
Q

second law of thermodynamics

A

all systems tend to entropy(chaos)

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9
Q

all systems tend to entropy unless

A

energy is being put in

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10
Q

transforming energy results in

A

loss of organized, usable energy as heat

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11
Q

1865 Philosophical Society of Zurich presentation Clausius concludes:

A

The entropy of the universe tends to a maximum.’

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12
Q

theClausius statement

A

Heat can never pass from a colder to a warmer body without some other change

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13
Q

Biological version

A

enzyme mediated chemical reactions cause the change that decreases the entropy of a substance

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14
Q

spontaneous processes occur on their own to

A

increase disorder

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15
Q

Heat flows from

A

high concentration of heat to low

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16
Q

The universe tends toward

A

chaos (entropy)

Second law

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17
Q

Without the input of E. disorder…

A

increases, dead things decompose

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18
Q

Solar E. is added to ecosystems via

A

photosynthesis

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19
Q

Conversion of E from one form to another results in

A

loss of usable energy in form of heat

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20
Q

only – percent of energy is passed up the food chain

A

10 percent

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21
Q

G stands for

A

free energy

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22
Q

change in G indicates

A

if a reaction will be spontaneous

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23
Q

negative ΔG

A

increases entropy
spontaneous
new molecules are lower E… degradative
exergonic pathway

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24
Q

Positive ΔG

A

decreases entropy = require an input of energy to occur (synthesizes molecules that are higher E)
endergonic pathway

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25
Q

ΔG = ΔH - T ΔS

A 
ΔH  = change in enthalpy
ΔS =  change in entropy
T = absolute Temperature in Kelvin
ΔG = change in Gibbs free energy
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26
Q

catabolism chart

A 
Degredative
Breaks down large mol.
Hydrolysis rxns
Increases entropy by
Releasing E. (- ΔG)
Exergonic
Cellular respiration
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27
Q

anabolism chart

A 
Biosynthetic
Builds large molecules
Condensation rxns
Decreases entropy by
Storing E in mol. (+ ΔG)
Endergonic
Photosynthesis
Refugees energy to work
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28
Q

Energy Coupling

A

Exergonic rxns power endergoninc rxns

Energy is transferred via ATP

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29
Q

Adenosine triphosphate

A

Nucleoside used in RNA (ribose + adenine (sugar and base)
Plus 3 phosphates
Hydrolysis (breaking) of ATP releases inorganic phosphate

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30
Q

inorganic phosphate

A

(Pi)+ 13 kcal/mol

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31
Q

Adenosine triphosphate Proteins can harness that E to

A 
transport molecules (protein pumps)
 move things ( motor proteins)
drive endergonic rxns
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32
Q

ATP drives endergonic rxns by

A

Substrate level phosphorylation

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33
Q

Substrate level phosphorylation

A

enzyme transfers one Phosphate from ATP to a molecule creating an Unstable intermediate

34
Q

Unstable intermediate

A

is a higher energy mol.

more likely to react spontaneously…releasing the Pi

35
Q

Glu + NH3= endergonic (+G)

A

So in body Glu forms an unstable phosphorylated intermediate first
Then the Pi is replaced
by the lower energy NH3
Combined the reactions
are exergonic (-G) & therefore spontaneous

36
Q

ATP moves proteins by

step one

A

ATP is hydrolyzed and protein is phosphorylated…then Pi is released result: protein changes its structure

37
Q

ATP moves proteins by

step two

A

ATP binds to protein …hydrolyzing ATP releases energy that causes protein to change shape

38
Q

Enzymes

A 
Proteins
Biological catalysts
Speed reactions but are NOT a reactant (not used up)
lower activation energy
do NOT alter overall ΔG
39
Q

a —– reaction requires a higher activation energy than does a—-

A

an uncatalyzed reaction requires a higher activation energy than does a catalyzed reaction

40
Q

is there a difference between free energy of catalyzed and uncatalyzed reactions

A

no,no difference between catalyzed and uncatalyzed reactions

41
Q

substrate

A

reactant enzyme binds

42
Q

active site

A

pocket where substrate fits into enzyme

43
Q

induced fit

A

alteration of substrate or active site to make a better fit between them

44
Q

Allosteric site

A

pocket other than active site where activators & inhibitors can bind

45
Q

Activators

A

increase the activity of enzyme … stabilize enzyme in active form

46
Q

inhibitors

A

block activity of enzyme

…stabilize enzyme in inactive form

47
Q

Activation Energy lowered by…

A

aligning molecules favorably
putting stress on bonds in molecule
creating favorable microenvironment

48
Q

Allosteric Regulator molecules all bind to

A

allosteric site

49
Q

activator molecules stabilize enzyme in

A

active form

50
Q

inhibitor molecules
stabilize enzyme
in

A

inactive form

51
Q

active sites based on

A

shape, size, pH, polarity, charge

52
Q

Substrate held in place by

A 
weak interactions
       (H-bonds, ionic bonds)
53
Q

enzymes catalyze

A

one reaction

54
Q

Competitive inhibitors

A

mimic substrate, bind active site covalently & inactivate enzyme

55
Q

Feed-Back Inhibition

A

allosteric
The end-product of a pathway shuts down the first enzyme of the pathway that creates it
prevents overproduction of products

56
Q

cofactors

A

Non-protein molecules/atoms needed for enzymes to work

57
Q

inorganic cofactors

A

Inorganic cofactors include Zn Fe & Cu ions

58
Q

Organic cofactors are

A

called coenzymes

include many vitamins & vitamin derivatives and nucleotides like NAD+ & FAD

59
Q

things that influence reaction rates

A

Concentration of enzymes/coenzymes/cofactors
pH
Temperature
Concentration of substrate
Concentration of allosteric molecules
Localization of reactions (compartmentalization)
Denatured enzymes or altered enzyme structure

60
Q

denatured

A

if temp and pH change beyond enzymes optimum, shape of enzyme changes, this affects the active site and means the enzyme will no longer work

61
Q

what does increasing temp do

A

Increases KE

Increases reaction rate

62
Q

Excessive Temperature denatures enzyme by

A

Breaking H bonds that

Hold enzyme in its secondary structure

63
Q

Does heat change chemical energy

A

No, only breaking bonds affects it

64
Q

Adding energy to ecosystems does what

A

Maintains order

65
Q

What is free energy

A

En hey that can perform energy, is available

66
Q

Order

A

Lots of energy in molecule

67
Q

Disorder

A

Less energy in molecule

68
Q

Exergonic pathway

A

Giving off energy kinda like expthermic

69
Q

Change in G is

A

Difference between what it starts with (products) and ends with (reactants)

70
Q

For exergonic reactions explain energy relationship

A

Reactants have more energy than products (lose energy)

71
Q

What is activation energy

A

The energy the reactants gain from the environment until the reaction can run

72
Q

Endergonic pathway

A

Put in energy

73
Q

Endergonic reaction reaction relationship with energy

A

Reaction energy is less than the products (gains energy)

74
Q

What increases enthalpy (order)

A

When increasing concentration and building bigger molecules

75
Q

What increase entropy

A

Spread molecules out and break them apart

76
Q

Which one is spontaneous: anabolic or catabolic

A

Catabolic

77
Q

What molecule is more stable

A

One with less energy

78
Q

Hydrolyzed ATP goes to

A

ADP+P

79
Q

If want to include an enzyme in a reaction put it where

A

Over the yield sign

80
Q

What is the only difference between catalyzed and uncatalyzed reactions

A

The activation energy

81
Q

How can competitive inhibitors be overcome

A

can be overcome by vast increase in substrate concentration

Ap Biology (33 decks)

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