quiz 3 Flashcards

(170 cards)

1
Q

What is thermodynamics

A

the study of energy and its transformations

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2
Q

what is the system and what is it called for things outside the system

A

system is the object under study and everything else is its surroundings

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3
Q

what are the three type of systems and describe them

A

isolated: system and surroundings does not exchange matter or energy
closed: only exchanges energy
open: exchanges energy and matter

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4
Q

name an example of an open system

A

Humans, organisms

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5
Q

What is the first law of thermodynamics

A

energy can be transformed from one form to another but it can’t be created nor destroyed

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6
Q

what is the second law of thermodynamics (2)

A

1) the total disorder (entropy) of a system and its surroundings always increase but the total energy of the universe does not change
2) Entropy of universe always increase

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7
Q

what is energy

A

the capacity to do work

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8
Q

what are the two states of energy and what is the difference

A

kinetic (energy of motion) and potential (stored energy)

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9
Q

name some forms of energy

A

chemical, thermal, electrical, radiant, mechanical

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10
Q

How (or to where) is energy transformed/transferred

A

energy is transferred between reactants and products, and between reactants or products and their surroundings.

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11
Q

What is the energy of reaction/ energy of formation

A

energy released or absorbed during chemical reaction

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12
Q

What is a spontaneous reaction

A

a chemical or physical reaction that will occur without an input of energy

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13
Q

what are two factors that determine whether a reaction is spontaneous or not

A

1) the change in energy content of a system

2) its change in entropy

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14
Q

Do reactions tend to be spontaneous when products have less potential energy than reactants or more PE?

A

reactions tend to be spontaneous when products have less potential energy than reactants

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15
Q

what is enthalpy and what is the variable assigned to it

A

Enthalpy is the potential energy in a system, (H)

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16
Q

When is a reaction exothermic

A

Reactions that release energy or when the products have less PE than reactants (Delta H is negative)

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17
Q

When is a reaction endothermic

A

Reactions that absorb energy or when products have more PE than reactants (Delta H is positive)

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18
Q

Reactions tend to be spontaneous if products are (more or less) ordered than the reactants

A

less ordered

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19
Q

Reactions tend to be spontaneous if products have (greater or lesser) entropy than the reactants

A

greater

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20
Q

What is gibbs free energy

A

the portion of a system’s energy that is available to do work

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21
Q

what is the equation of gibbs free energy

A
Delta G= Delta H - T(delta S)
Delta G is change in free energy
Delta H is change in enthalpy
T is temp in kelvin
Delta S is change in entropy
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22
Q

For a reaction to be spontaneous, Delta G must be (positive or negative)

A

Delta G must be negative

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23
Q

Name an example where a negative Delta H dominates making the reaction spontatneous

A

Combustion of methane (large loss of potential energy meaning negative enthalpy

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24
Q

Name an example where delta S dominates making the reaction spontaneous

A

Melting of ice at room temp, decrease in order dominates

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25
Fix this statement. | In many spontaneous biological reaction, reactants fully convert to products since the reaction has a negative delta G
In many spontaneous biological reaction, reactants may not fully convert to products even though the reactions have a negative delta G
26
What is the equilibrium point in a reaction
a state of balance between the opposing factors pushing the reaction in either directions
27
As a system moves toward equilibrium, what happens to free energy and delta G
free energy progressively lowers to its lowest point when system achieves equilibrium (delta G= 0)
28
Why is moving away from equilibrium not spontaneous
it requires free energy
29
When delta G is near 0, is the reaction reversible
yes
30
in a chemical equation, how are reversible reactions showed
double arrow
31
why do many reaction in living organism never reach equlibrium
because living systems are open and the supply of reactants is constant and products don't accumulate
32
why is delta g of life always negative
organisms constantly take in energy rich molecules and use them to do work
33
when do organisms reach equilibrium (delta G = 0)
only when they die
34
What is an exergonic reaction (3)
Reaction that releases free energy Delta G is negative because the products contain less free energy than reactants spontaneous reaction
35
what is an endergonic reaction (3)
reactants must gain free energy from surroundings to form products Delta G is positive because products contain more free energy than the reactants non spontaneous reaction
36
Define metabolic pathway
a series of reactions in which the products of one reaction are used immediately as reactants in the next reaction
37
Name the 2 different metabolic pathways
``` Catabolic pathway (or a single catabolic reaction) and anabolic pathway (anabolic reaction or biosynthetic reaction). Catabolic pathway is breakdown of complex molecules to simpler compounds (delta G is negative) Anabolic pathway is build of complicated molecules from simpler ones (delta G is positive) ```
38
What is the chief energy currency of the cell
ATP (adenosine triphosphate)
39
What is ATP composed of
ribose, adenine, and 3 phosphate group
40
where is the energy stored in ATP
in the high energy bonds between the phosphates
41
What is the purpose of ATP( other than being the primary energy currency)
ATP is used to drive endergonic reactions
42
What is made after hydrolysis reaction with ATP
ADP and a inorganic phosphate (Pi)
43
What is the delta G of ATP hydrolysis
-7.3 kcal/mol
44
ADP can be hydrolyzed into what
AMP
45
what is energy coupling
ATP hydrolyzed where the terminal phosphate group is transferred to a reactant molecule involved in endergonic reaction
46
What is phosphorylation
addition of a phosphate group to a molecule
47
What is a requirement for phosphorylation
An enzyme is needed with a specific site that binds both ATP and the reactant molecule to bring the two together
48
Is ATP synthesis an endergonic or exergonic reaction
Endergonic reaction
49
Where do we find the energy for ATP synthesis
energy from exergonic breakdown of carbohydrates, proteins, and fats (food)
50
Approximately how many ATP molecule are hydrolyzed and resynthesized each second in a typical cell
10 million
51
What is the ATP/ADP cycle
continual hydrolysis and resynthesis of ATP
52
What are redox reactions
Where oxidation and reduction occurs in a reaction | Electrons pass from one atom to another carry energy with them
53
what is oxidation and what is reduction
Oxidation is when an atom or molecule loses an electron | Reduction occurs when an atom or molecule gains an electron
54
T/F | A spontaneous reaction has a activation energy of 0
false
55
What is the variable assigned to activation energy
Ea
56
What is activation energy
The amount of energy needed to make bonds unstable (destabilize chemical bonds) and ready to be broken (the transition state)
57
What is a catalyst
substance that lowers the activation energy thereby accelerating the rate of reaction
58
What are enzymes
catalyst that cannot violate the law of thermodynamic
59
Do enzymes alter delta G of the reaction
no
60
How does an enzyme work in enzymatic reactions
enzymes combines briefly with reacting molecules and is unchanged when the reaction is complete
61
what is the reactant that an enzyme acts on called?
substrate
62
what is enzyme specificity
Each type of enzyme catalyzes the reaction of a single type of substrate or group of closely related molecules
63
What is an active site
a small pocket or groove in the enzyme that the substrate interacts with
64
what is induced fit
when the substrate binds at the active site, both enzyme and substrate molecules are distorted, making the chemical bonds in substrate ready for reaction (as opposed to lock and key model)
65
Once an enzyme substrate complex is formed, catalysis occurs- the substrate is converted into (how many products?)
one or more
66
which macromolecule do enzymes belong in
protein
67
Are enzymes consumed in a reaction
no, they are not consumed and can be reused so only a small amount is needed
68
What allows enzyme to stabilize a temporary association between substrates
unique 3d shape of enzyme (active site)
69
Cells have (how many) enzymes (inside, outside, or both) the cell
thousands, inside and outside
70
how do we know if something is an enzyme by its name and how do we know its respective substrate
the enzyme will end in -ase and refer to its substrate or type of reaction (maltase, amylase, proteinase, ribonuclease in ainfensens experiment, etc)
71
What is a cofactor
a nonprotein group that binds to the enzyme for catalytic activity. Some are metallic ions (iron, copper, magneisum, zinc, manganese)
72
what is a coenzyme
a cofactor that is a small organic molecule, which are often derived from vitamins
73
what is an example of a coenzyme
NAD/NADP
74
Name 3 major mechanisms that are part of enzymes that stabilize the transition state
1) bringing the reacting molecules together 2) exposing the reactant molecules to altered charge environment that promote catalysis 3) changing the shape of the substrate molecules
75
name 4 factors affecting enzyme activity
1) Concentration of substrate and other molecules that bind to enzymes 2) control mechanisms that modify enzyme activity (inhibitors) 3) temperature 4) pH- ionic interactions hold enzymes together
76
when enzyme concentration is kept constant, what happens to the rate of reaction as we increase substrate concentration
the rate of reaction will increase until it flattens out, this means the enzymes are saturated and the rate is solely dependent on the amount of enzyme molecules and how fast they work, no longer increase of substrate will increase rate
77
what are enzyme inhibitors
nonsubstrate molecules that bind to an enzyme and decrease its activity
78
what are competitive inhibitors
a inhibitor that competes with the substrate for the same active site
79
what are noncompetitive inhibitors
a inhibitor that binds at a site other than active site, causing the enzymes shape to change so that substrates can't bind to the active site
80
what is allosteric regulation and allosteric site
reversible binding of a regulatory molecule to the allosteric site (location on enzyme other than active site). Enzymes will have 2 alternate conformations: high affinity state (active) and low affinity state (inactive)
81
what is allosteric activation
an allosteric activator binds to an enzyme on the allosteric site and the enzyme goes from low affinity state to high affinity state
82
what is allosteric inhibiton
allosteric inhibitor goes into allosteric site and enzyme goes from high affinity state to low affinity state
83
what is negative feedback (feedback inhibition) and how is it related to allosteric inhibition
the product inhibits the process. The product is the allosteric inhibitor
84
What is regulation by chemical modification of an enzyme
chemical linkages to ions, functional groups, or other molecules that induce changes in enzyme that increase or decrease its activity
85
name an example of regulation by chemical modification of an enzyme
phosphorylation by protein kinases may activate or deactivate a protein
86
what do kinases do
transfer phosphate group from ATP to another molecule (kinase like kinetic energy??)
87
Typically, as temperature rises, how does the rate of reaction respond
rate of reaction typically increases
88
why can too high a temperature lower rate of reaction for an enzymatic reaction
kinetic motion increases and eventually hydrogen bonds break and the enzymes denature
89
What is optimum temperature
the ideal temperature for an enzyme where enzymatic activity is at its peak
90
what is the optimal pH of most enzymes
neutral, 7
91
what is the optimal pH of stomach enzymes (like pepsin)
acidic, 2
92
what is the RNA world
earliest forms of life might have inhabited RNA world, with no DNA or proteins to play critical roles. This is because ribozymes were informational molecules and had enzymatic function (could accelerate rate of certain biological reactions)
93
Name some functions of ribozymes (2)
cutting and splicing reactions that remove surplus segments from RNA molecules Catalyze linkage of amino acids in protein synthesis
94
What are autotrophs
Organisms that harvest sunlight and convert radiant energy into chemical energy
95
what are heterotrophs
organisms that live off the energy produced by autotrophs | extract energy from food via digestion and catabolism
96
what is cellular respiration
collection of metabolic reactions that breaks down food molecules to produce energy in the form of ATP (think mitochondria)
97
what is aerobic respiration and what organisms is it found in
form of cellular respiration in eukaryotes and many prokaryotes, oxygen is reactant in ATP producing process
98
what is anaerobic respiration and what organisms is it found in
form of cellular respiration found in some prokaryotes, molecule other than oxygen (sulfate or nitrate) is used in ATP producing process
99
what is the end goal of respiration
to produce ATP
100
is cellular respiration one redox reaction or many
many redox reactions
101
energy is released from oxidation in the form of what?
electrons
102
electrons are shuttled by electron carriers, name a electron carrier and where does it deliver to
NAD+ to an electron transport chain
103
at the electron transport chain, what happens
electron energy is converted to ATP
104
what is the final electron acceptor in aerobic respiration, anaerobic, and fermentation
oxygen for aerobic inorganic molecule for anaerobic organic molecule for fermentation
105
how do we obtain free energy for cellular work such as ATP synthesis in redox reactions
electrons release some of their energy as they pass from a donor molecule to an acceptor molecule
106
in redox reactions, do molecules only accept electrons? name an example or counter example
no they don't only accept electrons, they accept protons too. Oxygen accepts protons to make water
107
what is the standard chemical equation for making ATP from glucose. Is this aerobic or anaerobic? What is the delta G
C6H12O6 + 6O2 + 32ADP + 32Pi --> 6H2O + 6CO2 + 32ATP Aerobic -686kcal/mol
108
in aerobic respiration, can the large amount of energy be released at the same time?
no, it must be released in small steps
109
Are the electron carriers soluble or insoluble? Are they membrane bounded or not?
soluble and membrane bound
110
Are all carriers easily oxidized and reduced
yes
111
what do electron carriers carry
electrons, some can carry electrons and protons
112
what is the function of dehydrogenase enzyme
facilitate transfer of electrons from a fuel molecule to a molecule that acts as an electron carrier
113
what is the most common electron carrier
coenzyme nicotinamide adenine dinucleotide (NAD+)
114
in cellular respiration, what does the Dehydrogenase do to the NAD+
dehydrogenase transfers 2 electrons and 1 proton to NAD+ (oxidized form) to result into complete reduction to NADH (reduced form)
115
what does NAD+ and NADH have in common in structure? how are they different?
Both have adenine, 2 ribose and 2 phosphate groups, and nicotinamide. NAD+ has just 1 hydrogen bonded to the top carbon while NADH has 2 hydrogens connected to the top carbon
116
name the polymers of glucose that we need to know
glycogen, cellulose, and starch (and chitin if you want)
117
what are the 4 stages of oxidation of glucose in order and where in the cell does each occur
glycolysis (cytosol), pyruvate oxidation (mitochondrial matrix), krebs cycle (mitochondrial matrix), electron transport chain and Chemiosmosis (ATP production)(inner mitochondrial membrane)
118
in glycolysis enzymes break a (how many) carbon molecule of (what carbohydrate) into (what and how many)
enzymes break a 6 carbon glucose molecule into 2 3-carbon pyruvate molecules
119
what is substrate level phosphorylation
enzyme catalyzed reaction that transfers phosphate group from substrate to ADP
120
in pyruvate oxidation, enzymes convert what into what for the citric acid cycle
3-carbon pyruvate into a 2 carbon acetyl group
121
in the electron transport chain, electrons are delivered to what molecule and what is chemiosmosis established and what is it used for
electrons are delivered to oxygen by a sequence of electron carriers in the ETC free energy released by electron flow generates an H+ gradient by chemiosmosis and ATP synthase uses the H+ gradient as the energy source to make ATP
122
whats the equation for Calories in terms of proteins fats and carbs?
9(fat)+4(carbs)+4(proteins) all in grams
123
What is the difference between substrate level phosphorylation and oxidative phosphorylation
substrate level phosphorylation is transferring a phosphate group from the molecule directly to ADP oxidative phosphorylation is ATP synthase using energy from proton gradient
124
What is the chemical equation for glycolysis
Glucose + 2ADP + 2Pi + 2NAD+ + 4e- + 4H+ --> 2 pyruvate + 2ATP + 2 NADH + 2H+ + 2H2O
125
How much TOTAL ATP is made in glycolysis? How about NET ATP? How much NADH is made?
4 total, 2 net, 2NADH
126
what kind of transport moves pyruvate into the mitochondrial matrix
secondary active transport
127
pyruvate oxidation occurs where in eukaryotes and where in prokaryotes
mitochondria in eukaryotes and cytosol in prokaryotes
128
what is the equation for pyruvate oxidation for 1 glucose molecule (so start with 2 pyruvates)
2 pyruvate + 2CoA + 2NAD+ ---> 2acetyl-CoA + 2NADH + 2H+ +2CO2
129
what are other names of the citric acid cycle (2)
Krebs cycle, tricarboxylic acid cycle
130
what are the products of Krebs cycle for 1 glucose molecule
6NADH, 4CO2, 2FADH2, 2ATP, 6H+, 2CoA
131
what is needed for the first step of Krebs cycle
oxaloacetate, acetyl CoA and citrate synthase
132
What has glucose been oxidized to up till the end of Krebs cycle
6CO2, 4ATP, 10NADH, 2FADH2
133
What are some allosteric inhibitors for phosphofructokinase? (3), What activates it?
Excess ATP, Citrate, and NADH inhibit it. AMP activates it
134
What inhibits pyruvate kinase? (2), what activates it?
high levels of ATP and Acetyl CoA inhibits it. high levels of Fructose 1,6- bisphosphate activates it
135
What inhibits pyruvate dehrdrogenase
high levels of NADH
136
what inhibits citrate synthase (2)
high levels of ATP and citrate
137
what inhibits hexokinase
glucose 6 phosphate
138
what does ETC and ETS stand for
electron transport chain and electron transfer system
139
ETC is where?
embedded in the inner mitochondrial membrane
140
Which protein complex do electrons from NADH enter into? How about FADH2?
complex 1 for NADH and complex 2 to FADH2
141
where is the higher concentration and where is the lower concentration of protons
high H+ in intermembrane compartment and low H+ in matrix
142
what are the two small mobile electron carriers in the etc
cytochrome c and ubiquinone (coenzyme Q)
143
what are cytochromes
proteins with a heme prosthetic group that contains an iron atom to accept and donate electrons
144
are electron carriers organized from high to low free energy or low to high free energy
high to low free energy
145
what is the last terminal electron acceptor and what is it reduced to
O2 accepts 4 protons to turn into 2H2O
146
which protein complexes actively move protons
complexes 1 3 and 4
147
what kind of gradient is the proton gradient
electrical and chemical gradient
148
What is chemiosmosis/chemiosmotic hypothesis
that the proton gradient powers ATP synthesis by ATP synthase
149
Is the basal unit towards the intermembrane compartment or the matrix
towards the compartment, where protons can enter
150
What connects headpiece and basal unit
the stalk, a peripheral stator bridges the basal unit and headpiece
151
which part rotates in ATP synthase and in which direction
the basal unit rotates counterclockwise
152
What is the theoretical energy yield for bacteria and eukaryotes
38 ATP for bacteria and 36 ATP for eukaryotes
153
what is the theoretical yield of energy per NADH and FADH2
3 ATP for NADH and 2 ATP for FADH2
154
why does FADH2 make less ATP than NADH
FADH2 starts in complex 2
155
why does eukaryotes produce 2 less ATP than bacteria
Eukarya use 2 ATP to move the NADH in glycolysis in the cytosol to the matrix while prokaryotes everything happens in the cytosol
156
what is the actual yield of energy in bacteria and eukaryotes
32 ATP for prokaryotes and 30 ATP for eukaryotes per glucose
157
What is the actual yield of NADH and FADH2
2.5 ATP's for NADH and 1.5 ATP for FADH2
158
what causes the reduce yield of actual energy yield vs theoretical yield (2)
Leaky inner membrane where Protons move through other channels other than the ATP synthase use of proton gradient for other purposes other than ATP synthesis
159
Describe Racker and Stoeckenius experiment
they made a synthetic phospholipid membrane vesicles with a portion made of bacteriorhodopsin, a light activated proton pump, and ATP synthase. The ATP synthase was oriented so the headpiece was on the outside of the vesicle and added ADP and Pi to the medium. Results show that the light made a proton gradient and that gradient drove ATP synthase to make ATP.
160
how many protons and electrons are removed in a molecule when making NADH from NAD+
2 electrons and 2 protons
161
what did srikanth talk about siamese cats
near the nose and ears and paws , the enzyme that makes the dark pigment has optimal activity at lower temperatures, hence the different colors
162
what is phosphatase
enzyme that dephosphorylates
163
name an example of a reversible compeitive inhibitor
aspirin
164
aspiring inhibits what enzyme
cyclo-oxygenase
165
name an example of a irreversible compeitive inhibitor
pencillin
166
name an example of non compeitive inhibitor
cyanide
167
is dna negatively charged, why or why not
yes because of the phosphate group
168
name an example of a cell that is in g0
neurons
169
what is another name for anabolic pathway
biosynthetic reaction
170
do catalyst and enzymes increase rate of rxn
yes