Exam 2 Lecture 4 Flashcards

1
Q

All living systems
require an ongoing
supply of

A

energy

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2
Q

energy can be thought of as

A

the capacity to
cause specific chemical
or physical changes

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3
Q

Cells Need Energy to Drive 6 Different Kinds of
Work which are

A
  1. Synthetic work
  2. Mechanical work
  3. Concentration work
  4. Electrical work
  5. Generation of heat
  6. Generation of lig
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4
Q

synthetic work

A

changes in chemical Bonds
formation of Bonds

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5
Q

biosynthesis

A

The work of biosynthesis
results in the formation of new
chemical bonds and the
synthesis of new molecules
 Biosynthesis is required for
growth and maintenance of
cells and cellular structures
 Energy that cells require for
biosynthetic work is used to
make energy-rich organic
molecules and incorporate them
into macromolecules

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6
Q

Mechanical Work

A

Changes in the Location or
Orientation of a Cell or a Subcellular Structure

Mechanical work involves a
physical change in the position
or orientation of a cell or some
part of it
 The movement of a cell relative
to its environment often requires
one or more appendages, such
as cilia or flagella
 These require energy to move
the cell

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7
Q

Examples of mechanical work

A

A large number of muscle cells work together in
muscle contraction
 Chromosomes move along spindle fibers during
mitosis
 Cytoplasmic streaming and movement of
organelles and vesicles along microtubules occur
 Ribosomes move along a strand of mRNA

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8
Q

Concentration Work

A

Concentration work accumulates substances within a cell or
organelle or removes toxic by-products of cellular activity

Examples include the concentration of specific molecules and
enzymes in organelles, digestive enzymes in secretory
vesicles, and the import of sugars and amino acids into cells

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9
Q

Electrical Work

A

Moving Ions Across a
Membrane Against an Electrochemical Gradient

During electrical work, ions are transported across a
membrane, resulting in differences in both concentration and
electrical potential (or membrane potential)
 Every cellular membrane has a characteristic electrical potential
 In the case of mitochondria or chloroplasts, the difference is
essential in production of AT

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10
Q

Electrical work in Neurotransmission

A

Electrical work is important in transmission of nerve
impulses
 In this case, a membrane potential is generated by
pumping Na + ions into and K + ions out of the cell
 The electric eel (Electrophorus electricus) uses
energy to generate a membrane potential of 150
mV per cell and several hundred volts for the entire
organism

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11
Q

heat

A

an increase in temperature that is useful to warm-blooded Animals

Living organisms do not use heat as a form of energy as a steam engine does

However, producing heat is a major use of energy in all
homeotherms
 Homeotherms: animals that
regulate their body temperature
independent of the environment

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12
Q

Homeotherms:

A

animals that
regulate their body temperature
independent of the environment

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13
Q

Bioluminescence

A

the production of Light
Bioluminescence, the
production of light, is important
in a number of organisms, such
as fireflies, certain jellyfish, and
luminous toadstools
 Bioluminescence is generated
by the reaction of ATP with
luminescent compounds
 Green fluorescent protein (GFP;
from the jellyfish Aequorea
victoria) and its variants are
very useful to cell biologists

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14
Q

Nearly all life on Earth is directly or indirectly
sustained from

A

sunlight

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15
Q

phototroph

A

capture light energy from the sun and
transform it into chemical energy, stored as ATP

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16
Q

chemotrophs

A

obtain energy by oxidizing chemical
bonds in molecules (organic or inorganic)

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17
Q

Autotrophs

A

an organism that is able to form nutritional organic substances from simple inorganic substances such as carbon dioxide.

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18
Q

Heterotrophs

A

an organism deriving its nutritional requirements from complex organic substances.

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19
Q

Photoautotrophs

A

use solar energy to produce all the
carbon compounds they need from CO2
(photosynthesis)
 Photoautotrophs include plants, algae,
cyanobacteria, and photosynthetic bacteria

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20
Q

photoheterotrophs

A

Some bacteria are photoheterotrophs, which harvest
solar energy for some cellular activities but rely on
intake of organic molecules as a source of carbon

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21
Q

chemoautotrophs

A

A few bacteria are chemoautotrophs, which oxidize
inorganic compounds such as H 2S, H2, or inorganic
ions for energy and use CO 2 as a carbon source

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22
Q

Chemoheterotrophs

A

ingest and use chemical
compounds (carbohydrates, fats, and proteins) to
provide both energy and carbon for cellular needs
 All animals, protozoa, fungi, and many bacteria
are chemoheterotrophs

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23
Q

Energy Flows

A

Through the Biosphere
Continuously

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24
Q

Oxidation

A

is the removal of
electrons from a substance,
usually hydrogen atoms (H +
plus one electron)
 Oxidation reactions release
energy

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25
Q

reduction

A

Reduction, the addition of
electrons to a substance
through addition of hydrogen
atoms (and a loss of oxygen
atoms), requires an input of
energy

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26
Q

Phototrophs

A

the PRODUCERS, use sunlight energy to produce more reduced
cellular compounds through photosynthesis

These compounds are converted to all the materials needed for surviva

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27
Q

Chemotrophs

A

the CONSUMERS, take in reduced compounds and oxidize
them to release their stored energy

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28
Q

efficiency of Biological Processes

A

No process in biological systems is
100% efficient; some energy is inevitably released (lost) as heat,
usually dissipated into the
environment

Some of this heat is used
 In warm-blooded animals to
maintain body temperature
 In plants to attract pollinators or
melt overlying snow

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29
Q

The Flow of Energy Through the Biosphere Is
Accompanied by

A

a flow of matter

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30
Q

Energy enters the biosphere
as _______________ and leaves as _________ both without _________

A

Energy enters the biosphere
as photons and leaves as
heat, both without matter

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31
Q

while passing
through the biosphere,
energy exists primarily in the
form of

A

chemical bond
energies

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32
Q

matter cycles between

A

phototrophs and
chemotrophs

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33
Q

cyclic flow of matter includes

A

Carbon, oxygen, nitrogen,
and water all cycle
continuously
 They enter the
chemotrophic sphere as
reduced, energy-rich
compounds and leave it as
oxidized, energy-poor
forms

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34
Q

Energy flow is governed by the principles of

A

Thermodynamics

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35
Q

Thermodynamics

A

concerns the laws governing
energy transactions that accompany most
physical and chemical processes

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36
Q

Bioenergetics

A

(applied thermodynamics) applies
principles of thermodynamics to the biological world

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37
Q

Energy can be defined as

A

the ability to cause
change

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38
Q

The energy under consideration in any particular case is called the

A

system

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39
Q

the rest of the universe is called

A

the surrounding

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40
Q

The boundary between the system and
surroundings may be

A

real or hypothetical

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41
Q

A closed system is

A

sealed
from its environment and can
neither take in nor release
energy

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42
Q

An open system

A

can have
energy added to it or
removed from it

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43
Q

Organisms are what type of system

A

open
systems, capable of uptake
and release of energy

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44
Q

A system is in a specific

A

state if each of its variable properties is held at a
specified value.
 In this situation, the total energy of the system has a unique value.
 If the state changes, the total energy change is determined only by the
initial and final states of the system

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45
Q

what are three of the most important variables in biological reactions

A

Three of the most important variables—temperature, pressure, and
volume—are essentially CONSTANT during biological reactions.

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46
Q

why are temp, pressure, and volume essentially constant during bio rxn

A

This is because reactions occur in dilute solutions within cells at
approximately the same temperature, pressure, and volume during the
entire reaction.

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47
Q

Oil Rig

A

Oxidation is losing
reduction is gaining

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48
Q

Exchange of energy between a system and its
surroundings occurs as

A

Heat or work

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49
Q

is heat a useful energy source for cells?

A

Heat is not a very useful energy source for cells
because many biological systems are isothermal
(at a fixed temperature)

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50
Q

work is

A

the use of energy to drive a process other than heat flow

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51
Q

The units for quantifying the energy changes during
chemical reactions are

A

calories (cal) (1 kilocalorie (kcal)
= 1000 calories).

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52
Q

Physicists prefer the

A

joule (J); 1 J = 0.239 cal

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53
Q

calorie

A

the amount of energy required to raise 1 gram of
water by 1 degree centigrade at 1 atmosphere of pressure

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54
Q

first law of thermodynamics

A

the law of
conservation of energy.
 It states that in every physical or chemical change, the
total amount of energy in the universe remains constant.
 Energy may be converted from one form to another but
cannot be created or destroyed

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55
Q

In biological systems, the energy that leaves a system
must

A

equal that which entered it plus the amount
remaining (stored) in the system

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56
Q

Total energy stored within a system is called

A

internal
energy, or E.

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57
Q

ΔE is the

A

change in internal energy that occurs during
some process

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58
Q

Calculating ΔE

A

ΔE is the difference in internal energy of a system before a
process (E1 ) and after it (E2 )
2 1E E E  
 For a chemical reaction, this can be written as
products reactantsE E E  

( see slide)

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59
Q

Enthalpy

A

change in enthalpy (H),
or heat content, which is related to E, dependent on
pressure (P) and volume (V)
 H = E + P V

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60
Q

Enthalpy in biological processes

A

Enthalpy change of a particular reaction can be
expressed as:
 Because pressure and volume change little or not at all in
biological reactions,
ΔH may be either positive or negative

see slide for equation

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61
Q

Exothermic rxn

A

ΔH is negative

In exothermic reactions, energy is released (e.g., the
burning of gasoline in a car)

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62
Q

If ΔH is positive, a reaction is

A

endothermic

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63
Q

In endothermic rxn energy is

A

Absorbed
( melting of an ice cube)

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64
Q

The Second Law of Thermodynamics
States That Reactions Have

A

directionality

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65
Q

A thermodynamically spontaneous reaction is

A

one that is a
favorable reaction.

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66
Q

Thermodynamic spontaneity

A

is a measure of whether or
not a reaction or process can occur

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67
Q

Reactions have directionality, that is

A

they can proceed
spontaneously only in one direction (e.g., the burning of a
piece of paper).

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68
Q

The second law of thermodynamics is the law of

A

thermodynamic spontaneity

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69
Q

thermodynamic spontaneity

A
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70
Q

first law

A

heat
enthalpy

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71
Q

second law

A

order

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72
Q

second law explained

A

in every physical or chemical change, the
universe tends toward greater disorder or randomness
(entropy).
* It allows us to predict what direction a reaction will
proceed under specific conditions, how much energy will
be released, and how changes in conditions will affect it

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73
Q

Entropy and Free Energy Are Two
Alternative Means of Assessing

A

Thermodynamic Spontaneity

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74
Q

Whether or not a reaction can proceed can be measured
by changes in

A

entropy or free energy

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75
Q

Entropy (S) is a measure of

A

randomness or disorder
All processes or reactions that occur spontane (??)

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76
Q

when a system becomes less ordered entropy …

A

Increases
(e.g., when ice melts or a solvent evaporates)

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77
Q

when a system becomes more ordered

A

Entropy decreases
ex. when ice forms water

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78
Q

Entropy Change as a Measure of

A

Thermodynamic Spontaneity

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79
Q

change in S universe is positive for

A

or every spontaneous process or
reaction (increases the entropy of the universe)

But in the specific system involved, entropy may change
or stay the same.
 Expressing the second law in terms of ΔS is not very
useful in predicting the spontaneity of biological
processes.

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80
Q

A measure of spontaneity for a system alone is called

A

free energy (G)

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81
Q

change in free energy equation

A

Gproducts - Greactants

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82
Q

ΔG is related to

A

enthalpy and entropy of a reaction

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83
Q

ΔG = ( in terms of enthalpy and entropy )

A

ΔG = ΔH − T ΔS (T = temperature of the system in
degrees Kelvin, or C +273)

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84
Q

Free energy is a readily measurable indicator of

A

spontaneity

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85
Q

Every spontaneous reaction is characterized by a______ in free energy of the system

A

decrease

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86
Q

So, if ΔG < 0, the reaction is

A

thermodynamically
spontaneous.

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87
Q

thermodynamically
spontaneous rxn

A

ΔG < 0

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88
Q

Exergonic rxn are

A

Exergonic reactions are energy-yielding and occur spontaneously
(ΔG < 0)

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89
Q

endergonic rxn are

A

Endergonic reactions are energy-requiring and do not occur
spontaneously under the conditions specified (ΔG > 0)

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90
Q

is the oxidation of glucose exergonic or endergonic

A

the oxidation of glucose (a highly
exergonic process):
6 12 6 2 2 2C H O + 6O 6CO + 6H O + energy

ΔG = −686 kcal/mol

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91
Q

the reverse rxn of glucose oxidation is exergonic or endergonic ?

A

The reverse reaction is endergonic ( input of energy)

ΔG = +686 kcal/mole

6CO + 6H O + energy C H O + 6O2

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92
Q

The term spontaneous tells us that

A

a reaction can take
place, not that it will

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93
Q

Whether an exergonic reaction will proceed depends on

A

on a
favorable (negative) ΔG but also on the availability of a
mechanism.
 Usually an input of activation energy is required as well

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94
Q

equilibrium constant

A

Keq

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95
Q

Keq

A

is the ratio of product
concentrations to reactant concentration at equilibrium.
 At equilibrium, there is no net change in the
concentrations of reactants or products

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96
Q

keq equation

A

keq = [B]/[A]

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97
Q

what can the equilibrium constant tell you about a mixture

A

If you know the equilibrium constant for a reaction, you
can tell whether a particular mixture of products and
reactants is in equilibrium.

 If the mixture is not at equilibrium, you can tell in what
direction it must proceed to reach equilibrium

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98
Q

what is the concentration ratio

A

the ratio of products to reactants

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99
Q

what does it mean when the concentration is less than Keq ?

A

A concentration ratio (products to reactants) less than Keq
means that the reaction will proceed to the right to
generate more product

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100
Q

what does it mean when the concentration is MORE than Keq ?

A

A concentration ratio greater than Keq means that the
reaction will proceed to the left ( toward reactants)

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101
Q

ΔG is

A

free energy change
in cal/mol

102
Q

R is
( when calculating ΔG)

A

R is the gas constant
(1.987 cal/mol × K

103
Q

T is
( when calculating ΔG)

A

is the temperature in
kelvins

104
Q

Keq is equilibrium constant
at standard temperature of

A

298 K (25C)

105
Q

In stands for

A

natural log

106
Q

Know how to calculate ΔG

A

see slides on page 16

107
Q

what are the limitations on ΔG

A

it tells us nothing about rate or mechanism of
the reaction

108
Q

ΔG is a thermodynamic parameter that tells us

A

whether a
reaction is thermodynamically possible as written
and It also tells us how much free energy would be liberated if
the reaction took place

109
Q

what are the conditions called for ΔG is made

A

Biochemists have agreed on conditions to define the
standard state.
25C (298 K), 1 atmosphere
pressure, and all products

reactants at a
concentration of 1.0 M
standard pH = 7.0
the concentration of H + and OH− ions is 10^−7

110
Q

is water included when calculations of free energy change

A

The concentration of water is not included in calculations
of free energy change

111
Q

why are Keq and ΔG written with a′ ?

A

to indicate standard
conditions: K′eq and ΔG′

112
Q

in any thermodynamic parameter, the standard change
refers to

A

The conversion of one mole of a specified reactant to
product or
 The formation of one mole of a specified product from
the reactants
 The free energy change calculated under these conditions
is called the standard free energy change (ΔGº′

113
Q

what is the relationship between ΔGº′ and ln K′eq???

A

Linear relationship
This means that ΔGº′ can be calculated directly from the
equilibrium constant, provided Keq was determined under
the same standard conditions

114
Q

If K′eq is greater than 1.0, then ΔGº′

A

will be negative, and the
reaction can proceed to the right (toward the products) under
standard conditions

115
Q

If K′eq is less than 1.0, then ΔGº′

A

will be positive, and the
reaction will tend toward the left (toward the reactants) under
standard conditions.

116
Q

what is important to know about ΔGº′

A

ΔGº′ is an arbitrary standard, referring to impossible
conditions for most biological systems

117
Q

what is ΔG′ most useful?

what information does it provide

A

For real life situations, ΔG′ is the most useful measure of
thermodynamic spontaneity

ΔG′ provides a measure of how far from equilibrium a
reaction is, under the conditions in a cell

118
Q

what does ΔG′ = 0 mean

A

the reaction is in
equilibrium; however, reactions in living cells are rarely in
equilibrium

119
Q

red blood cell, actual concentrations are

A
120
Q

jumping beans

A

Jumping beans are seeds of certain shrubs with moth
larvae inside.
 When the larva moves, the seed moves too

see slides with example

121
Q

ΔG =
( equation)

A

= ΔH – T(ΔS)

122
Q

ΔG and the Capacity to Do Work

A

The change in Gibbs energy is equal to the maximum amount of work that a system can perform on the surroundings while undergoing a spontaneous change (at constant temperature and pressure

in bean example The greater the difference in free energy between the two
chambers, the more work the system can do

123
Q

work can be performed continuously

A

work can be performed continuously as long
as equilibrium is never reached

124
Q

how do cells lower activation energy barrier

A

using catalysts called enzymes

125
Q

does ΔG discuss rate

A

only how much energy is released

126
Q

Rate depends on

A

the height of the barrier between the two chambers

127
Q

Life is possible because cells maintain

A

in steady state,
with most reactions far from equilibrium

128
Q

A cell at equilibrium would be

A

DEAD

129
Q

At equilibrium, the forward and backward rates are

A

the same, and there is no net flow of matter

130
Q

Life Requires Steady-State Reactions
That

A

Move Toward Equilibrium
Without Ever Getting There

131
Q

why is steady state possible in cells?

A

Steady state is possible only because a cell is an open
system.
 It receives energy from the environment.
 Reactants and products of cellular chemistry are kept far
from equilibrium

132
Q

Enzyme catalysis

A

nearly all cellular reactions
involve protein catalysts called enzymes

 The presence of the appropriate enzyme
makes the difference between whether a
reaction can take place and whether it will take
place

133
Q

Activation Energy and the Metastable State

A

Many thermodynamically feasible reactions in a cell
that could occur do not proceed at any appreciable
rate
 For example, the hydrolysis of ATP has
ΔG = –7.3 kcal/mol
ATP + H2O ADP + Pi
 However, ATP dissolved in water remains stable
for several days

134
Q

The presence of the appropriate enzyme
makes the difference between

A

whether a
reaction can take place and whether it will take
place

135
Q

what prevents molecules from reacting

A

lack of sufficient energy

136
Q

what is activation Energy?

A

the minimum amount of energy required before
collisions between the reactants will give rise to
products

137
Q

what is a transition state?

A

Reactants need to reach
an intermediate
chemical stage called
the transition state
 The transition state has
a higher free energy
than that of the initial
reactants

138
Q

The rate of a reaction is
always proportional to

A

the
fraction of molecules with
an energy equal to or
greater than EA

139
Q

The only molecules that
are able to react at a
given time are

A

those with
enough energy to exceed
the activation energy
barrier, EA

140
Q

The Metastable State Is a Result of

A

the Activation Barrier

141
Q

what does metastable
state

A

Reactants that are thermodynamically unstable, but
lack sufficient EA

142
Q

Life depends on high activation energies that
prevent

A

most reactions in the absence of catalysts

prevents so many reactions from taking place and over working the cell?

143
Q

most reactions in the absence of catalysts

A

activation energy barrier

144
Q

what are the two ways Ea can be overcome

A

The EA barrier must be overcome in order for
needed reactions to occur
 This can be achieved by either increasing the
energy content of molecules or by lowering the EA
requirement

145
Q

how can you increase the energy content of a system

A

The input of heat can
increase the kinetic
energy of the average
molecule, ensuring that
more molecules will be
able to take part in a
reaction

also think of mixing sugar and water

146
Q

is increasing heat helpful in cells? why or why not?

A

no because cells are Isothermal

147
Q

Isothermal

A

constant in temperature

148
Q

How can Activation Energy be lowered

A

If reactants can be bound on a surface and brought close
together, their interaction will be favored and the required EA
will be reduced
 A catalyst enhances the rate of a reaction by providing such a
surface and effectively lowering EA
 Catalysts themselves proceed through the reaction unaltered

149
Q

what are the three basic properties of catalysts

A

hey increase reaction rates by lowering the
EA required
2. They form transient, reversible complexes with
substrate molecules
3. They change the rate at which equilibrium is
achieved, not the position of the equilibrium

150
Q

organic catalysts are

A

Enzymes

151
Q

most enzymes are

A

proteins

However, recently it has been discovered that
some RNA molecules also have catalytic activity
 These are called ribozymes

152
Q

Ribozymes

A

RNA molecules with catalytic activity

153
Q

what is an active site

A

Every enzyme contains a characteristic cluster of amino acids
that forms the active site

  • directly involved in the action

This results from the three-dimensional folding of the protein
and is where substrates bind and catalysis takes place
 The active site is usually a groove or pocket that
accommodates the intended substrate(s) with high affinity

154
Q

which amino acids are involved in active sites

A

These are cysteine, histidine, serine, aspartate,
glutamate, and lysine

 These can participate in binding the substrate and
several serve as donors or acceptors of protons

155
Q

Cofactors

A

Some enzymes contain nonprotein cofactors
needed for catalytic activity, often because they
function as electron acceptors
 These are called prosthetic groups and are
usually metal ions or small organic molecules
called coenzymes
 Coenzymes are derivatives of vitamins

156
Q

what a re prosthetic Groups

A

Prosthetic groups are located at the active site and
are indispensable for enzyme activity

( normally metal ions?)

Each molecule of the enzyme catalase has a multimeric
structure called a porphyrin ring to which a necessary
iron atom is bound
 The requirement for certain prosthetic groups on
some enzymes explains our requirements for trace
amounts of vitamins and minerals

157
Q

Substrate specificity

A

Because of the shape and
chemistry of the active
site, enzymes have a very
high

158
Q

inorganic catalysts are

A

very nonspecific

159
Q

Group specificity o

A

Some enzymes will accept a number of closely
related substrates
 Others accept any of an entire group of substrates
sharing a common feature
 This group specificity is most often seen in
enzymes involved in degradation of polymers

160
Q

6 major classes of Enzymes

A

Oxidoreductases
 Transferases
 Hydrolases
 Lysases
Isomerases
 Ligases
see table for more
knwo how they function and the differences between them

161
Q

how are enzymes characterized

A

by their sensitivity to
temperature

This is not a concern in homeotherms—birds and
mammals—which maintain a constant body
temperature
 However, many organisms function at their
environmental temperature, which can vary widely

162
Q

At higher temperatures, the rate of enzyme activity

A

inecreases with temperature as a result of increased
kinetic activity of enzyme and substrate molecules

However, beyond a certain point, further increases
in temperature result in denaturation of the enzyme
molecule and loss of enzyme activity

163
Q

the reaction rate of human enzymes is maximum at what temp and what is this called?

A

37 C
(the
optimal temperature), the normal body temperature

164
Q

Most enzymes of homeotherms are inactivated by temperatures

A

above 50–55º

165
Q

Enzymes of cryophilic

A

(cold-loving) organisms such
as Listeria bacteria can function at low
temperatures, even under refrigeration

166
Q

General pH range for enzymes

A

Most enzymes are active within a pH range of about 3–4 units

167
Q

pH dependence is usually due to

A

the presence of charged
amino acids at the active site or on the substrate

168
Q

pH changes affect

A

the charge of such residues and can disrupt
ionic and hydrogen bonds

169
Q

what else are enzymes sensitive to

A

Enzymes are sensitive to factors such as molecules
and ions that act as inhibitors or activators
 Most enzymes are also sensitive to ionic strength of
the environment
 This affects hydrogen bonding and ionic
interactions needed to maintain tertiary
conformation

170
Q

why are enzymes highly specific

A

Because of the precise chemical fit between the
active site of the enzyme and its substrates,
enzymes are highly specific

171
Q

substrate binding

A

Once in the active site, substrate molecules are
bound to the enzyme surface in the right orientation
to facilitate the reaction
 Substrate binding usually involves hydrogen bonds,
ionic bonds, or both
 Substrate binding is readily reversible

172
Q

The Induced-Fit Model

A

In the past, the enzyme was seen as rigid, with the
substrate fitting into the active site like a key in a lock
(lock-and-key model)
 A more accurate view is the induced-fit model, in
which substrate binding at the active site induces a
conformational change in the shape of the enzyme

173
Q

conformational change

A

The induced conformational change brings needed amino acid
side chains into the active site, even those that are not nearby
 Once in the active site, the substrate is held in place by specific
noncovalent interactions
 These position the substrate optimally for catalysis and
distinguish the real substrate from similar molecules

174
Q

The role of the active site is

A

to recognize and bind
the appropriate substrate and also to activate it by
providing the right environment for catalysis

This is called substrate activation, which
proceeds via several possible mechanisms

175
Q

Three Common Mechanisms of Substrate
Activation

A

Bond distortion, which makes the bond more
susceptible to catalytic attack
 Proton transfer, which increases reactivity of
substrate
 Electron transfer, which results in temporary
covalent bonds between enzyme and substrate

176
Q

The Catalytic Even

A

the sequence of events

The random collision of a substrate molecule with the
active site results in its binding there
2. Substrate binding induces a conformational change that
tightens the fit, facilitating the conversion of substrate into
products
3. The products are then released from the active site
4. The enzyme molecule returns to the original conformation,
and the active site is now available for another molecule of
substrate

177
Q

Ribozymes

A

Are Catalytic RNA Molecules
 Catalytic RNA molecules were discovered in the
1980s
 These are called ribozymes
 Many scientists believe that the earliest enzymes
were catalytic, self-replicating RNA molecules

178
Q

Tetrahymena RNA

A

ITetrahymena RNAIn 1981 Thomas Cech and colleagues discovered
an RNA molecule that was self-splicing
 This is an example of autocatalysis

179
Q

Ribonuclease P

A

is an enzyme that cleaves transfer
RNA precursors to yield functional RNA molecules
 Ribonuclease P has an RNA and a protein
component
 In the early 1980s, Sidney Altman showed that only
the RNA component was capable of performing the
cleavage

180
Q

Ribosomes

A

Ribosomes synthesize proteins. They have protein and RN
A components.
 The active site of the large subunit of a ribosome is the
site of peptidyl transferase activity, the catalysis of the
peptide bond.
 The ribosomal RN A (rRNA) is the catalyst.
 The rRNA is a ribozyme

181
Q

The rRNA is a

A

ribozyme

182
Q

Enzyme kinetics

A

describes the quantitative
aspects of enzyme catalysis and the rate of
substrate conversion into products

183
Q

Reaction rates are influenced by factors such as

A

the concentrations of substrates, products, and
inhibitors

184
Q

initial Reaction Rates

A

Initial reaction rates are measured over a brief time,
during which the substrate concentration has not
yet decreased enough to affect the rate of reaction

185
Q

Monkey Peanut

A

see slides

186
Q

[S]

A

substrate concentration - concentration rep by brackets

187
Q

how does increase the substrate concentration increase in the cell

A

faster the time to find the substrate decreases but with diminishing returns

the only way to increase rate is to increase enzyme concentration

188
Q

Initial reaction velocity (v0)

A

the
rate of change in product
concentration per unit time depends on the substrate
concentration ([S]).

189
Q

at low [S], doubling [S] will affect Vo by …

A

double v0 ; but as [S] increases,
each additional increase in [S]
results in a smaller increase in v0

190
Q

When [S] becomes very large,
the value of v0 reaches a

A

Maximum

191
Q

As [S] tends toward infinity, v approaches an upper limiting
value

A

maximum velocity (Vmax)

192
Q

The value of Vmax can be increased by

A

adding more
enzyme

193
Q

saturation

A

The inability of increasingly higher substrate
concentrations to increase the reaction velocity beyond a
finite upper value is called saturation

194
Q

who postulated a theory of enzyme action and what is it

A

Michaelis and Menten

Substrate (S) is catalyzed by enzyme (E) to produce
product (P)

195
Q

The Michaelis–Menten Equation

A

see slides/ anki

196
Q

what is a rate constant

A

A rate constant is the proportionality constant relating the
rate of a reaction to the concentrations of reactants

197
Q

What Is the Meaning of Vmax and Km?

A

We can understand the relationship between v0 and [S],
and the meaning of Vmax and Km (the Michaelis constant)
by considering three cases regarding [S]:
1. Very low substrate concentration
2. Very high substrate concentration
3. [S] = Km

reference slides

198
Q

At very low [S], the initial velocity of the reaction is roughly

A

proportional to the substrate concentration, [S].

199
Q

At very high [S], the initial velocity of the reaction is

A

ndependent of variation in [S], and Vmax is the velocity at
saturating substrate concentrations.

200
Q

Vmax

A

Vmax
 Vmax is the upper limit of v0
as the substrate
concentration [S]
approaches infinity.
 It is the velocity at
saturating
concentrations
The Linear Relationship Between
Vmax and Enzyme Concentration
 Vmax is an upper limit
determined by:
 The time required for
the actual catalytic
reaction
 How many enzyme
molecules are present
 The only way to increase
Vmax is to increase enzyme

201
Q

The lower the Km value for a given enzyme and substrate,

A

the lower the [S] range in which the enzyme is effective

202
Q

Vmax is important as a measure of the

A

potential maximum
rate of the reaction.

203
Q

By knowing Vmax , Km, and the in vivo substrate
concentration, we can estimate

A

the likely rate of the
reaction under cellular conditions

204
Q

turnover number

A

see slide

205
Q

The Double-Reciprocal Plot Is a Useful
Means of Visualizing Kinetic Data

A

see slide

206
Q

what can influence enzymes

A

Enzymes are influenced (mostly inhibited) by products,
alternative substrates, substrate analogues, drugs, toxins,
and allosteric effectors

207
Q

what is a vital control of mechanisms in cells

A

inhibition

208
Q

inhibitor important to enzymologists and why are they important

A

substrate analogues and transition state
analogues

transition state analogue
- analogues - mimic

These are compounds that resemble real
substrates or transition states closely enough to
occupy the active state but not closely enough to
complete the reaction

209
Q

transition state analogue

A

transition state analogs have some structural characteristics that are unique to the transition state

210
Q

substrate analogue

A

substrate analogs mimic the structural features of the substrates

Substrate analogues are important tools in fighting
infectious diseases

211
Q

Irreversible inhibitors, + examples

A

bind the enzyme
covalently, cause permanent loss of catalytic
activity and are generally toxic to cells
 Examples: heavy metal ions, nerve gas poisons,
some insecticides

212
Q

Reversible inhibitors and what are the two forms

A

bind enzymes noncovalently
and can dissociate from the enzyme
The fraction of enzyme available for use in a cell
depends on the concentration of the inhibitor and
how easily the enzyme and inhibitor can dissociate
 E + I EI
 The two forms of reversible inhibitors are
competitive inhibitors and noncompetitive
inhibitors

213
Q

Competitive Inhibition
what is it ? function?

A

Competitive inhibitors bind the active site of an enzyme and so compete with
substrate for the active site
 Enzyme activity is inhibited directly because active sites are bound to
inhibitors, preventing the substrate from binding

( similar structure to the substrate )

214
Q

Noncompetitive Inhibition
what is the inhibitor and its funtion

A

Noncompetitive inhibitors bind the enzyme molecule outside the active site
 They inhibit activity indirectly by causing a conformation change in the
enzyme that
 Inhibits substrate binding at the active site, or
 Reduces catalytic activity at the active site

215
Q

HIV treatment

A

target specific enzymes within a pathway by knowing the structure of the enzyme such that you can make a substrate analogue to prevent the rxn from taking place
see image for details

216
Q

difference between reversible and irreversible inhibitor binding to enzyme

A

irreversible bind to the enzyme COVALENTLY
reversible bind to the enzyme NONcovalently

217
Q

process of noncompetitive inhibition

A

get info from slide

218
Q

why is enzyme regulation important and how does it occur

A

Enzyme rates must be continuously adjusted to
keep them tuned to the needs of the cell
 Regulation that depends on interactions of
substrates and products with an enzyme is called
substrate-level regulation
 Increases in substrate levels result in increased
reaction rates, whereas increased product levels
lead to lower rates

219
Q

how can cells turn enzymes on and off as needed by
two mechanisms?

A

allosteric regulation and covalent
modification
 Usually enzymes regulated this way catalyze the
first step of a multistep sequence
 By regulating the first step of a process, cells are
able to regulate the entire process

220
Q

Allosteric regulation

A

is the single most important
control mechanism whereby the rates of enzymatic
reactions are adjusted to meet the cell’s needs

  • see pathway on slide

need a diff enzyme for each step to produce the next substrate needed for the following step

221
Q

Feedback Inhibition

A

It is not in the best interests of a
cell for enzymatic reactions to
proceed at the maximum rate - too much energy and too much waste

 In feedback (or end-product)
inhibition, the final product of
an enzyme pathway negatively
regulates an earlier step in the
pathway

see pathway on slide

222
Q

what are the two conformations of allosteric enzymes needed for regulation

A

one
in which it has affinity for the substrate(s) and one
in which it does not
 Allosteric regulation makes use of this property
by regulating the conformation of the enzyme
 An allosteric effector regulates enzyme activity by
binding and stabilizing one of the conformations

223
Q

allosteric regulation

A

makes use of this property
by regulating the conformation of the enzyme

224
Q

allosteric effector

A

regulates enzyme activity by
binding and stabilizing one of the conformations

binds a site called an
allosteric (or regulatory) site, distinct from the
active site

225
Q

an allosteric effector may be an

A

activator or
inhibitor, depending on its effect on the enzyme

226
Q

Inhibitors shift the equilibrium between the two
enzyme states to the

A

low-affinity form

227
Q

low-affinity form

A

high-affinity form

228
Q

describe the process of allosteric inhibition

A

an enzyme subject to allosteric inhibition is active …. pg 51

229
Q

describe

A
230
Q

describe the structure of allosteric enzymes

A

large, multisubunit
proteins with an active or allosteric site on each
subunit

231
Q

where are active and allosteric sites located

A

Active and allosteric sites are on different subunits,
the catalytic and regulatory subunits,
respectively

232
Q

what does the binding of allosteric effectors affect the subunits

A

Binding of allosteric effectors alters the shape of
both catalytic and regulatory subunits

233
Q

Allosteric Enzymes Exhibit_____________ interactions between subunits

A

cooperative

234
Q

Many allosteric enzymes exhibit

A

cooperativity

235
Q

what is cooperativity of enzymes?

A

As multiple catalytic sites bind substrate molecules, the
enzyme changes conformation, which alters affinity for the
substrate.
 In positive cooperativity, the conformation change
increases affinity for substrate; in negative cooperativity,
affinity for substrate is decreased

236
Q

In positive cooperativity, the conformation change

A

increases affinity for substrate

237
Q

in negative cooperativity,
affinity for substrate is

A

decreased

238
Q

what is covalent modification

A

Many enzymes are subject to covalent modification.
 Activity is regulated by addition or removal of groups, such
as phosphate, methyl, and acetyl groups

^ form of regulation

239
Q

covalent modification example

A

The reversible addition of phosphate groups is a common
covalent modification

240
Q

Phosphorylation

A

the addition of a phosphoryl group
and occurs most commonly by transfer of a phosphate
group from ATP to the hydroxyl group of serine, threonine,
or tyrosine residues in a protein

241
Q

Protein kinases

A

catalyze the phosphorylation of other
proteins.

242
Q

Dephosphorylation

A

the
removal of phosphate groups
from proteins, is catalyzed by
protein phosphatases

Depending on the enzyme,
phosphorylation may be
associated with activation or
inhibition of the enzyme

243
Q

Fisher and Krebs won the
Nobel Prize for their work on

A

glycogen phosphorylase

244
Q

what is Glycogen
Phosphorylase?

A

allosteric enzyme

245
Q

What are the two interconvertible forms of glycogen phosphorylase?

A

An active, phosphorylated form (glycogen phosphorylase
a)
 An inactive, nonphosphorylated form (glycogen
phosphorylase b)

246
Q

what are the enzymes responsible for regulation of glycogen phosphorylase?

A

Phosphorylase kinase phosphorylates the enzyme
 Phosphorylase phosphatase removes the phosphate

247
Q

proteolytic cleavage

A

The activation of a protein by a one-time, irreversible removal of
part of the polypeptide chain is called proteolytic cleavage

248
Q

Proteolytic enzymes of the pancreas

A

trypsin, chymotrypsin,
and carboxypeptidase—are examples of enzymes synthesized
in inactive form (as zymogens) and activated by cleavage as
needed.

249
Q

enzymes can inhibit completely or

A

reduce rate

250
Q

allosteric site is also called

A

regulatory site

251
Q

is is not a general rule that

A

phosphorylation activates and dephosphorylation deactivates - it depends ont he enzyme

252
Q

trypsin
slides on 53

A

an enzyme that aids with digestion. An enzyme is a protein that speeds up a certain biochemical reaction.