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AP Biology > Ch 8 > Flashcards

Ch 8 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

metabolism

A

the totality of an organisms chemical reactions

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2
Q

metabole

A

greek for change

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3
Q

metabolism is a(n) ______ property

A

emergent

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4
Q

a metabolic pathway begins with-

A

a specific molecule

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5
Q

mechanisms that regulate___ balance metabolic supply and demand

A

enzymes

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6
Q

metabolism manages

A

the material and energy resources of a cell

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7
Q

degradative metabolic pathways which release energy by breaking down complex molecules to simpler compounds

A

Catabolic pathways (also called break down pathways)

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8
Q

A major pathway of catabolism

A

cellular respiration

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9
Q

catabolism in cellular respiration

A

the sugar glucose and other organic fuels are broken down in the presence of oxygen to carbon dioxide and water

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10
Q

Pathways can have _____ starting molecule and/or product

A

more than one

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11
Q

energy that was stored in organic molecules…

A

becomes available to do the work of the cell

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12
Q

anabolic pathways (also called biosynthetic pathways)

A

metabolic pathways consume energy to build complicated molecules from simpler ones

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13
Q

examples of anabolism

A

synthesis of amino acids and proteins from amino acids

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14
Q

bioenergetics

A

the study of how energy flows through living organisms

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15
Q

energy

A

the capacity to cause change

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16
Q

kinetic energy

A

energy associated with the relative motion of objects

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17
Q

heat or thermal energy

A

kinetic energy associated with the random movement of atoms or molecules

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18
Q

a type of energy that can be harnessed to perform work

ex.photosynthesis

A

light

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19
Q

potential energy

A

energy that matter possesses because of its location or structure ; energy that is not kinetic

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20
Q

potential energy examples

A

water behind a dam, molecules due to their structure

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21
Q

chemical energy

A

potential energy available for release in a chemical reaction

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22
Q

complex molecules, such as glucose

A

are high in chemical energy

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23
Q

when kinetic energy is converted into potential energy a small amount of energy

A

is lost as heat due to friction

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24
Q

thermodynamics

A

the study of energy transformations that occur in a collection of matter

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25
Q

surroundings in thermodynamics

A

everything outside the system (the rest of the universe)

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26
Q

system in thermodynamics

A

the matter under study

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27
Q

isolated system

A

is unable to exchange either energy or matter with its surroundings

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28
Q

open system

A

energy and matter can be transferred between the system and its surroundings

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29
Q

organisms are ____ systems (in thermodynamics)

A

open

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30
Q

first law of thermodynamics (principle of conservation of energy)

A

energy can be transferred and transformed, but it cannot be created or destroyed

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31
Q

entropy

A

a measure of disorder, or randomness

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32
Q

second law of thermodynamics

A

every energy transfer or transformation increases the entropy of the universe

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33
Q

spontaneous (energetically favorable) process

A

a process that can occur without an input of energy; must increase entropy of the universe

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34
Q

nonspontaneous process

A

energy must be added

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35
Q

energy flows into most ecosystems as light

A

and leaves as heat

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36
Q

the entropy of a particular system, such as an organism, may decrease as long as

A

the total entropy of the universe (system and surroundings) increases

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37
Q

Gibbs free energy of a system (G), free energy

A

portion of a system’s energy that can perform work when pressure and temperature are uniform throughout a system (a cell for example)

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38
Q

(change in free energy calculation)

A

Delta G = Delta H - T Delta S

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39
Q

Delta (change in free energy calculation)

A

a triangle (letter in greek alphabet)

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40
Q

Delta H (change in free energy calculation)

A

change in system’s enthalpy

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41
Q

enthalpy

A

equivalent to total energy in biological systems

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42
Q

delta S (change in free energy calculation)

A

change in system entropy

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43
Q

T (change in free energy calculation)

A

absolute temperature in Kelvin

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44
Q

Kelvin

A

K=C+ 273

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45
Q

only processes with a negative delta G

A

are spontaneous

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46
Q

for delta G to be negative

A

either delta H must be negative and/or T delta S must be positive

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47
Q

difference between free energy of initial state and free energy of final state

A

delta G= G(final state)-G(initial state)

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48
Q

unstable systems have

A

higher G

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49
Q

stable systems have

A

lower G

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50
Q

equilibrium

A

state of maximum stability

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51
Q

most chemical reactions are reversible and proceed to a point where

A

forward and backward reactions occur at the same rate

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52
Q

at equilibrium

A

G is at its lowest possible value

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53
Q

any change away from equilibrium

A

has a positive effect on G and will not be spontaneous

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54
Q

systems___ move spontaneously move away from equilibrium

A

never

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55
Q

a system at equilibrium cannot

A

do work

56
Q

a process is spontaneous and can perform work only when

A

it is moving towards equilibrium

57
Q

exergonic reaction

A

energy outward, net release of energy, loses free energy, delta G is negative, spontaneous

58
Q

endergonic reaction

A

energy inward, absorbs free energy from surroundings, G increases, delta G is positive, nonspontaneous, and delta G’s magnitude=energy required to drive reaction

59
Q

cellular respiration formula

A

C6H1206+602=6CO2+6H20

60
Q

the breaking of bonds

A

requires energy

61
Q

in an isolated system reactions will

A

reach equilibrium and cannot do work

62
Q

if metabolism were isolated

A

it would reach equilibrium

63
Q

cells don’t reach equilibrium because

A

of the constant flow of materials

64
Q

key to prevent equilibrium

A

reaction product does not accumulate

65
Q

The cell does 3 kinds of work

A

chemical-pushing of endergonic reactions that would not occur spontaneously, ex. polymer synthesis, transport-pumping substances across membranes against spontaneous movement direction, and mechanical-cilia beating, muscle contraction, chromosome movement in cell reproduction

66
Q

energy coupling

A

using exergonic processes to drive endergonic ones

67
Q

main mediator of energy coupling and acts as immediate source of energy in most cases, that powers cellular work

A

ATP

68
Q

ATP

A

adenosine triphosphate

69
Q

ATP contains

A

the sugar ribose, nitrogenous base adenine and a chain of three phosphate groups bonded to it

70
Q

ATP phosphate bonds can be broken by

A

hydrolysis

71
Q

in the cell most hydroxyl groups of phosphates are

A

ionized (-O-)

72
Q

ATP hydrolysis

A

ATP+H2O= AN INORGANIC PHOSPHATE,ADP, and releases energy

73
Q

energy in the hydrolysis of ATP comes from

A

lowering of free energy

74
Q

all 3 phosphate groups in ATP are ___ charged

A

negatively

75
Q

with what can a cell use ATP energy for things other than heat (such as driving reactions normally endergonic)

A

enzymes

76
Q

if delta G of an endergonic reaction is less than the amount of energy released by hydrolysis ,than

A

the two reactions can be coupled so that , overall, the coupled reaction are exergonic, usually uses a phosphorylated intermediate

77
Q

phosphorylated intermediate

A

the recipient of a transfer of a phosphate group from ATP: phosphate group is covalently bonded to it.

78
Q

how is ATP regenerated

A

the addition of phosphate to ADP

79
Q

the free energy required to phosphorylate ADP comes from

A

exergonic catabolism (breakdown reaction)

80
Q

ATP cycle

A

the shuttling of inorganic phosphate and energy

81
Q

the regeneration of ATP is inherently

A

endergonic

82
Q

ATP cycle is incredibly

A

fast

83
Q

to form ATP what is required other than a phosphate and ADP

A

free energy from catabolic pathways; cellular respiration and plants use light

84
Q

enzyme

A

a macromolecule which acts as a catalyst, a chemical agent that speeds up a reaction without being consumed by the reaction

85
Q

spontaneous reactions like glucose in sterile water can be

A

imperceptibly slow

86
Q

activation energy (free energy of activation))

A

initial investment energy-energy required to contort the reactant molecules so that bonds can break

87
Q

were does activation energy often come from

A

thermal energy in the surroundings

88
Q

unstable condition when molecules have absorbed enough energy for bonds to break

A

transition state

89
Q

there must be enough energy in an exergonic reaction

A

to reach the transition state

90
Q

many molecules in the human body are prone to decomposing spontaneously, why don’t they

A

few molecules can make it over the activation hump at cell temperature

91
Q

an enzyme catalyzes by

A

lowering the activation energy barrier, enabling the reactant molecules to absorb enough energy to reach the transition state even at moderate temperatures

92
Q

an enzyme CANNOT change

A

the delta G for a reaction: cannot make an endergonic reaction exergonic

93
Q

enzymes can only hasten reactions which

A

would occur anyway

94
Q

dynamic metabolism

A

the routing of chemicals smoothly through the cell’s metabolic pathways due to enzymes

95
Q

because enzymes are specific for the reactions they catalyze

A

they determine which chemical processes will be going on in the cell at any particular time

96
Q

substrate

A

the reactant an enzyme acts on

97
Q

enzyme-substrate complex

A

an enzyme bound to its substrate (or substrates when there are two or more reactants)

98
Q

enzyme-substrate process

A

enzyme+ substrate(s)=enzyme-substrate complex=enzyme+ product(s) via catalytic action of the enzyme

99
Q

most enzyme names end in

A

-ase

100
Q

an enzyme can recognize its

A

specific substrate, even among closely related compounds

101
Q

the specificity of an enzyme results from its

A

shape, which is a consequence of its amino acid sequence

102
Q

active site

A

the restricted region of the enzyme molecule that actually binds to the substrate, typically a pocket or groove on the surface of the enzyme where catalysis occurs , usually only formed by a few of the enzymes amino acids. with the rest of the protein providing a framework that determines the configuration of the active site

103
Q

an enzyme is not

A

a stiff structure locked into a given shape

104
Q

enzymes “dance” between

A

subtly different shapes in a dynamic equilibrium with slight differences in free energy for each pose

105
Q

the shape that best fits the substrate isn’t necessarily

A

the one with the lowest energy, but during the short time the enzyme takes on this shape, its active site can bind to the substrate

106
Q

the active site is

A

not a rigid receptacle of the substrate

107
Q

induced fit

A

the active site changes shape slightly to fit substrate due to interaction between the chemical groups. This brings them into positions which that enhance their ability to catalyze the chemical reaction

108
Q

in most enzymatic reactions the substrate is held in place by

A

hydrogen and ionic bonds

109
Q

what part of the active site catalyzes

A

the R groups of a few amino acids

110
Q

enzymes are (speed)

A

fast

111
Q

since most metabolic reaction are reversible

A

enzymes can catalyze either forward or the reverse reaction depending on negative delta G, which depends on reactant-product concentrations, with a net effect towards equilibrium

112
Q

enzymes use a variety of mechanisms to lower activation energy. name them

A

1, in reactions containing two or more reactants, a template is provided for them to come together in proper orientation

  1. enymes may stretch substrate toward transition state, stressing and bending critical chemical bonds
  2. active sight can provide environment more conductive to a particular reaction
  3. direct participation of the active sight in the reaction, sometimes even involves covalent bonding of amino acids in enzyme to substrate
113
Q

saturated enzyme

A

enough substrate so that all active sites are engaged

114
Q

factors controlling rate of substrate to product conversion (excluding enzyme activity factors)

A
  • amount of substrate in solution (pre-saturation)

- amount of enzyme (post saturation)

115
Q

what controls enzyme activity factors

A
  • general environmental factors such as pH and temperature

- chemicals that influence the enzyme

116
Q

optimal conditions

A

when the enzymes work at their best

117
Q

to a point, rate of enzymatic reaction increases

A

with increasing temperature, however above a certain temperature this rate drops

118
Q

optimal temperature

A

temperatures where enzymes each work at their best

119
Q

optimal pH

A

best pHs for each enzymes

120
Q

cofactors

A

non-protein helpers for catalytic activity, organic or non-organic, tightly bound or bound loosely

121
Q

coenzyme

A

organic cofactor

122
Q

inhibitor is usually irreversible if

A

covalently bonded

123
Q

competitive inhibitors

A

bind to enzymes reversibly with weak interactions and resemble the normal substrate; thus they compete for admission into activation site

124
Q

how do you counter competitive inhibitors

A

add more substrate

125
Q

noncompetitive inhibitors

A

impede enzymatic reaction by binding to another part of the enzyme and thus lowers the efficacy of the activation site

126
Q

selective inhibition

A

inhibitors which regulate enzyme reactions naturally

127
Q

mutation

A

a permanent change in a gene, which can result in a protein with one or more changed amino acids

128
Q

if all of a cell’s metabolic pathways were operating simultaneously

A

chemical chaos would ensue

129
Q

how does a cell regulate where and when its various enzyme are active (and thus its metabolic pathways)

A

by switching genes off and on that control specific enzymes or by regulating enzyme activity once made

130
Q

allosteric regulation

A

any case where a protein’s function at one site is affected by binding a regulatory molecule to a separate site which may result in either inhibition or stimulation

131
Q

most enzymes known to be allosterically regulated are constructed from

A

two are more subunits, each composed of a polypeptide chain with its own active site

132
Q

the complex an allosterically regulated oscillate between

A

two different shapes, one catalytically active and the other inactive

133
Q

where is a regulatory or allosteric site often located

A

where subunits join

134
Q

what happens when an inhibitor and activator respectively bind to a regulatory sight

A

activator-stabilizes the shape that has functional active sites
inhibitor-stabilizes the inactive form of the enzyme

135
Q

explain ATP regulation

A

ATP-binds to several catabolic enzymes allosterically, lowering their affinity for substrate and thus inhibiting their activity
ADP-functions as an activator for same enzymes

136
Q

cooperativity

A

a substrate molecule binding to one active site in a multisubunit enzyme triggers a shape change in all the subunits

137
Q

feedback inhibition

A

a metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway

AP Biology (13 decks)

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