Section 1: Bioenergetics Flashcards

1
Q

Formation of polymers

A

Forms through dehydration (- H2O)
Breaks through hydrolysis (+ H2O)

Constructed of monomers

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2
Q

How much of the body is occupied by polymers?

A

~80%

The remaining 20% of a cell are monomers and other small molecules

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3
Q

Types of polymers

A

Lipids
Polysaccharides (carbohydrates)
Proteins
Nucleic acid

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4
Q

Building block of lipids

A

Acetates, which join tgt to form acyl chains

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5
Q

Lipids and phosphate

A

Lipids can grow to form hydrophobic fatty acid (acyl) chains

Addition of phosphate makes fatty acids amphipathic

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6
Q

Acyl chains can be…

A

Saturated or unsaturated

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7
Q

Lipids - functions

A
Energy storage (mass, energy of glycogen, a complex storage sugar)
Structural molecules (membranes)
Steroids (all from cholesterol, some further made into electron carriers and vitamins)
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8
Q

Lipids: Structure of a fat molecule

A

Ester linkages, which link glycerol and acyl chains together

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9
Q

The cell membrane is formed of a…

A

Phospholipid bilayer

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10
Q

Phospholipids - replication

A

No genetic info required, just physical laws of stability of vesicle size
Could have been the first form of replication

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11
Q

How are sugars formed

A

From central pathways (trioses)

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12
Q

Monosaccharides

A

Single sugars

Different types

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13
Q

Disaccharides and oligosaccharides

A

Form from several mixed sugar types

Disaccharide: 2 sugar molecules

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14
Q

How are polysaccharides formed

A

Formed from many repeated sugar units connected by glycosidic bonds
Specific glycosidic bonds determine flexibility

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15
Q

Polysaccharides - function

A
Energy storage (starch and glycogen)
Structural molecules - used by plants and animals to form structures, e.g. cellulose, chitin
Carbohydrate residues can be joined to proteins or lipids (glycoproteins/lipids)
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16
Q

Starch

A

A storage polysaccharide in plants
Polymer of glucose monomers
Stored as granules in plastids, e.g. chloroplasts

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17
Q

Glycogen

A

Sugar storage in animals
Polymer of glucose monomers - more extensively branched than starch –> more flexible with α 1-4 bonds
Large stores in liver and muscle cells

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18
Q

Cellulose

A

Structural polysaccharide in plants
Polymer of glucose (not branched)
Stored in cell wall
Most abundant organic compound on Earth

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19
Q

α vs β glycosidic bonds

A

α1–>4: starch and glycogen
β1–>4: chitin and cellulose

Subtle difference, but profound effect

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20
Q

Chitin

A

Structural polysaccharides in animals
Polymer of glucose, but glucose monomer has a N containing appendage
Forms exoskeleton of arthropods and fungi cell walls

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21
Q

Nucleic acids (RNA and DNA) - function

A

Involved in all informational processes
Storage of chemical energy in ATP
Intracellular signalling cAMP

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22
Q

Phosphodiester bond

A

PO4 3-

Formation leads to elimination of H2O (i.e. dehydration)

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23
Q

Components of nucleic acids

A

Sugar-phosphate backbone (phosphate group and sugar)
Nitrogenous base
5’ and 3’ end

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24
Q

Types of nitrogenous bases

A

Pyrimidines:
Cytosine (C)
Thymine (T in DNA)
Uracil (U in RNA)

Purines:
Adenine (A)
Guanine (G)

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25
Sugars - DNA vs RNA
One of the Hs in deoxyribose (in DNA) is replaced by OH in ribose (in RNA)
26
How are proteins formed
Formed from amino acids connected through peptide bonds | Bonds formed through dehydration and break through hydrolysis
27
Properties of proteins determine...
Protein structure and function
28
Parts of an amino acid
Amine group Carboxy terminus R side group
29
Life and order
Life generates order (decreases entropy) and drives itself away from equilibrium, but at the expense of making more disorder (increasing entropy)
30
Passage of energy
Photoautotrophs capture electromagnetic energy of light and converts this to chemical energy Heterotrophs consume, use and store chemical energy and pass energy onto carnivores At each passage of energy, some is lost to the universe as heat
31
Stored energy (via anabolic processes)
Occurs through synthesis of carbohydrates, fats, and proteins These are then catabolised (oxidised) to release energy O2 required to completely oxidise foodstuffs to CO2 and H2O
32
Where is energy conserved from oxidation reactions
Within phosphate bonds of ATP
33
What does ATP stand for
Adenosine triphosphate
34
Excess dietary fuel
Exceeds body's immediate energy needs Stored mainly as glycogen and fat Provides energy when fasting Oxidation of these fuels release energy, which often use Acetyl-Co Enzyme A
35
Gibb's free energy - equation
ΔG = ΔH - TΔS ΔH (enthalpy) = q + w (aka heat + work done) T (temperature) ΔS (entropy)
36
ATP
Almost universal - cells also use GTP, UTP and creatine phosphate Likely ancestral High ΔG --> can make the unfavourable favourable (spontaneous) Much higher tendency for ATP --> ADP + Pi than the other way around
37
How does ATP release energy
From electrically charged phosphates, which change molecular properties and do work
38
ATP phosphates
Electrical charges are crowded among phosphates, especially the terminal phosphate --> leaves more easily and can bind and carry with it the electrical charge This charge can then alter the conformation of a protein, altering the protein elsewhere In the cell, most hydroxyl groups of phosphates are ionised (O-)
39
Two fundamental laws of thermodynamics
1. Energy is not created nor destroyed, it just changes form 2. The overall entropy of the universe is increasing These laws are the foundation of Gibb's equation
40
Universe tends toward...
Disorder More disorder --> increased entropy (rotting apple) - exothermic More disorder --> going towards equilibrium
41
When a reaction reaches equilibrium...
They go no further
42
Anabolic processes
Build things up
43
Heat
The end result of all processes | Dissipates into the universe
44
Negative ΔG
The more -ve the ΔG, the greater the likelihood a reaction occurs
45
When is most ΔG in ATP released
Hydrolysis of ATP to ADP and inorganic phosphate ΔG of ATP is greater than the sum of 'products of formation' of ADP + Pi --> can drive rxns that would otherwise go too slowly or not at all
46
Anabolic vs catabolic processes
Anabolic: creates molecules the body needs for functionality and uses energy in the process Catabolic: breaks down complex molecules and releases energy which is available for the body to use
47
Example of anabolic vs catabolic processes
Anabolic: photosynthesis in chloroplasts ---organic molecules + O2---> cellular respiration in mitochondria Catabolic: cellular respiration in mitochondria ---CO2 + H2O---> photosynthesis in chloroplasts
48
Combustion of different food sources
Diff food sources release diff amounts of energy when combusted ``` Least to most: Carbohydrate Protein Alcohol Fat ```
49
Metabolism of different food sources
``` Least to most: Alcohol Fat Protein Carbohydrate ```
50
Why is combustion different to metabolism
Access to C-C bonds, internal and not easily accessed Metabolic enzymes work on C-H and O-H bonds Molecules must be rearranged
51
Fat
May have less energy for outright mass, but stores well and has no associated water Can't be metabolised without O2
52
Stages of catabolism
1. Hydrolysis of complex molecules to their building blocks 2. Conversion of building blocks to Acetyl CoA 3. Oxidation of acetyl CoA - oxidative phosphorylation
53
Acetyl-CoA
Hub molecule
54
ATP - structure
Phosphoanhydride bond - relatively stable in water | Phosphate group has resonance / charge delocalisation
55
Equilibrium vs non-equilibrium
``` Equilibrium = less order = higher entropy Non-equilibrium = ordered = low entropy ``` Life fights equilibrium/entropy
56
ΔG - purpose
Predicts whether a rxn occurs spontaneously Predicts max possible change in conc between reactants and products Does NOT predict rate at which reactions will occur
57
What does the ° mean in ΔG°
Standard conditions 1 mol/L, pH 7, 25°C In real life, these conditions are quite different - ΔG is maybe -50-60 kJ/mol
58
Exergonic reactions
Releases energy
59
Hydrolysis is dependent on..
Ratio of reactants to products | So, ATP is held at a high conc, and there is more reserve ATP
60
Human heart - ATP
Contains approx 700mg of ATP - enough to fuel one heartbeat per second for 10s
61
Formation of glutamine
1. ATP phosphorylates glutamic acid, making the amino acid less stable 2. Ammonia displaces phosphate group, forming glutamine Note: enzyme glutamine synthetase required Net ΔG is -ve
62
Does glycolysis require oxygen
No It is an initial component of aerobic metabolism, but can also operate without oxygen by fermentation to produce lactate or ethanol, but inefficient
63
Glycolysis enzymes
Enzymes of glycolysis are arranged to form pathways, which increases efficiency of reactions 10 enzymes produce 2 ATP net
64
Two phases of glycolysis
``` Energy investment (-2 ATP): - Hexo/Glucokinase - PFK Energy harvesting (+4 ATP): - Phosphoglycerate kinase - Enolase ```
65
Important features of glycolysis
Sugar-splitting reaction Oxidative event that generates reduced NADH Two specific steps where the reaction sequence is coupled to ATP generation by substrate-level phosphorylation
66
Glycolysis - steps
1. Conversion of glucose to glucose-6-phosphate (G6P) --> traps glucose --> can't be transported out of cells - irreversible Catalysed by hexokinase and glucokinase Requires energy (2 ATP invested) 2. G6P rearranged, and another phosphate is invested 3. Resulting intermediate then split into 2 molecules of the 3-carbon compound glyceraldehyde 3-phosphate 4. Each glyceraldehyde 3-phosphate molecule has an additional phosphate added alongside the formation of NADH (by reduction of NAD+) 5. 1, 3-bisphosphoglycerate is formed In following reactions, 4 ATP are recaptured by substrate level phosphorylation and 2 pyruvate molecules are formed
67
Glycolysis - Hexokinase vs glucokinase
Both interact with glucose, but in slightly diff ways Puts a phosphate on the glucose Hexokinase: Expressed in all tissues High affinity (low Km) for glucose At very low glucose conc, will already start to add a phosphate to it to form G6P (very sensitive to glucose) Glucokinase: Found predominantly in liver (takes up glucose and stores) and pancreatic beta cells (regulates insulin) Lower affinity (higher Km by ~100x) Must get up to a reasonable (higher) conc of glucose for it to work - high Vmax
68
Glycolysis - net reaction
Glucose + 2NAD+ + 2Pi + 2ADP --> 2pyruvate + 2NADH + 2H+ + 2ATP + 2H2O
69
Stages of cellular respiration
Glycolysis - breaks down glucose into 2 pyruvate molecules Citric Acid Cycle - completes breakdown of glucose Oxidative phosphorylation - accounts for most of the ATP synthesis
70
Lactate
End product of glycolysis during strenuous exercise | Lactate produce in muscle and other tissues can return to liver where it is reconverted to glucose - Cori cycle
71
For sustained flow of glycolysis...
NAD+ must be regenerated Anaerobic: NAD is regenerated by LDH (lactate dehydrogenase)
72
Glycolysis: Re-oxidation of NADH
Cells with O2: accomplished by oxidative phosphorylation Aerobic conditions: O2 may be limiting and ATP demands can exceed capacity of mitochondria Pyruvate is reduced to lactate by lactate dehydrogenase in cytosol
73
Glycolysis: Speed and efficiency
Can form ATP very quickly, but not very efficient as it only forms 2 ATP net per glucose (3 ATP if it comes from glycogen
74
Redox reactions
Oxidation: loss of electrons Reduction: gain of electrons
75
Oxidation of C bonds
Energy from C-C = C-H bonds, but C-C can't be oxidised directly Must be rearranged to C-OH for oxidation --> electrons ultimately flow to oxygen
76
Redox reactions use...
Dehydrogenases
77
Energy release must be...
Controlled, otherwise explosions! | Thus cellular respiration is controlled energy captured in ATP
78
Glycolysis: NAD+
Acts as an electron shuttle | Water soluble
79
Glycolysis: Irreversible enzymes
Hexokinase or glucokinase Phosphofructokinase Pyruvate kinase Highly regulated and irreversible in vivo
80
Glycolysis: At which point is glucose fully committed?
Phosphofructokinase (PFK) Highly regulated point in pathway (most important regulator) Another ATP invested
81
Glycolysis: What is PFK regulated by
High ATP slows down (ATP --> ADP -->) AMP activates PFK Citrate inhibits PFK from CAC Moderately low pH turns PFK on, but when too acidic inhibits PFK --> tight control
82
Energy yield of glycolysis vs aerobic glucose oxidation
Energy yield of aerobic glucose oxidation much greater
83
Main functions of CAC cycle
Oxidise acetyl-CoA Reduce co-enzymes NADH and FADH2 Form ATP (and decrease ADP) Therefore, principle driving forces for CAC is due to amount of reduced coenzymes and ADP abundance
84
CAC: Pyruvate (from glycolysis) is converted to...
Acetyl CoA, in an oxidative decarboxylation reaction by the pyruvate dehydrogenase complex Then further oxidised to CO2
85
CAC: Acetyl CoA is produced in most pathways of...
Fuel oxidation
86
Coenzymes
Complex organic structures, which participate in enzymatic reactions
87
CAC: Coenzymes
Coenzyme A, NAD+ and FAD
88
CAC: NAD+ vs FAD
Both are oxidation reduction coenzymes Both act as electron acceptors FAD able to accept single electrons and bound NAD+ is mobile in aqueous environment and accepts 2 e- in one step FAD has less reducing power
89
Where do most enzymatic reactions of CAC cycle occur
Mitochondrial matrix or bacterial cytosol
90
CAC: Oxidation reactions
4, which transfer electrons to NAD+ or FAD by binding Hs to form NADH + H+ and FADH2 Other reactions in the pathway result in rearrangements to facilitate REDOX reactions with NAD+ or FAD
91
CAC: Oxaloacetate
Regenerated in CAC after oxidation of NAD+ and FAD | Available to react with another molecule of acetyl CoA
92
Net energy yield from CAC and oxidative phosphorylation
High | ~10ATP for each acetyl group oxidised
93
Energy yield from oxidation of NADH and FADH2 by electron transport and phosphorylation systems
~2.5 ATP per NADH oxidised | ~1.5 ATP per FADH2 oxidised
94
The high-energy phosphate bond of GTP is generated by...
Substrate level phosphorylation
95
How does CAC 'control' ATP utilisation
ATP:ADP ratio Reduction state as per the NADH/NAD+ ratio (REDOX state) - high NADH = lots of reducing power Calcium (signal that indicates cells are depolarised/activated and need ATP)
96
CAC: Examples of key regulatory enzymes
``` Isocitrate dehydrogenase (IDH) α-ketoglutarate dehydrogenase (αKDH) ```
97
CAC: During oxidation of each molecule of acetyl CoA...
Only one molecule of high-energy phosphate (GTP/ATP) is produced
98
CAC equation for 2 pyruvates
6CO2, 8NADH, 2FADH2, 2GTP (or 2ATP)
99
Endosymbiosis
A symbiotic relationship where one organism lives inside the other
100
Mitochondria
Permits an existence with oxygen (quite toxic and in effect ages us) Allowed larger cells - cristae increase efficiency of ATP synthesis --> increases cell's capacity to make ATP --> more complex genomes --> increased gene copy numbers --> possibly drove rapid diversification of genes, cell structures, types and body plans
101
Junction between glycolysis and CAC
Irreversible step | Very large -ΔG and regulated
102
Vitamin B1 - Thiamine
Has thiamine pyrophosphate found within pyruvate dehydrogenase TPP is within E1 - acts to remove CO2
103
CAC: GTP vs ATP
Liver makes GTP, muscle makes ATP
104
CAC: Succinate dehydrogenase (SDH)
Part of ETS Complex II FAD+ bound within it Sits in inner mitochondrial membrane Directly connects oxidation to electron transfer
105
CAC: Amphibolic
Involves both catabolism and anabolism
106
CAC: If there is too much succinyl-CoA or acetyl-CoA...
CoA becomes limiting and CAC slows
107
CAC: ADP/ATP ratio regulates...
IDH activity 10/2 goes faster 2/10 goes slower
108
CAC: Ca2+ regulates...
PDH, aKDH and IDH
109
Cholesterol is an important component of...
Animal cell membranes
110
Glucose + glucose -->
Maltose + water (via dehydration)
111
Enzymatic reactions involved in glycolysis fatty acid breakdown and CAC cycle conserve most energy into _____
NADH and FADH2, which can transfer their electrical power into usable energy by transferring H+ across membranes
112
Respiratory complexes
Enzymes that sit on membranes and mediate H+ transfer as electrons from NADH and FADH2 ultimately flow to O2 and reduce it to form H2O
113
Electron transport system - gradients
H+ accumulates on one side of membrane --> generates gradient, which is harnessed to synthesize ATP
114
Oxidation of NADH and FADH2 results in...
Release of electrons
115
What is the electron transport system (ETS)
A sequence of electron-transfer carriers involving electrophilic molecules, e.g. flavins, haeme and iron-sulfur complexes, which transfer electrons in a step-wise manner to O2
116
ETS: The flow of electrons changes...
The charges of ETS protein complexes so they pump H+ or promote chemical reactions that transfer
117
ETS: Where are protons transferred
Across the inner mitochondrial membrane (IMM) from matrix to intermembrane space (IMS) --> raises pH in matrix and lowers it in IMS Therefore, there is a pH gradient and electrical potential
118
Electron transport carriers that oxidise NADH
``` Organised into three large membrane spanning complexes: Complex I (CI, aka NADH dehydrogenase) Complex III (aka cytochrome b-c1) Complex IV (aka cytochrome oxidase) ``` Together form super-complexes / respirosome Arranged as 3 separate units, but linked functionally by two additional electron carriers; co-enzyme Q and protein cytochrome C
119
Co-enzyme Q
A lipid soluble molecule (not a protein)
120
Electrons flowing through the NADH pathway drive...
Proton pumps of complex I and IV, and the chemical transfer of protons at complex III All develop a H+ gradient
121
Electron transport carriers that oxidise FADH2
Mediated by a second electron transport linked to CII Part of CII is succinate dehydrogenase (SDH), which is what FADH2 is bound to and most likely stops dangerous free radical production Flow from FADH2 (oxidised to FAD) and are transferred to co-enzyme Q --> electrons flow through complexes III and IV
122
ETS: Do electrons flow from CI to CII
No
123
Succinate dehydrogenase (SDH)
An enzyme of CAC
124
NADH vs FADH2 - redox potential
FADH2 has lower redox potential / reducing power | This means that CII itself doesn't pump protons, but CIII and CIV (downstream) still contribute to proton gradient
125
ETS: Flavin mononucleotide (FMN)
Specific molecule found within complexes I-IV which act as electron acceptors Made from vitamin B2 Top part similar to FAD (alloxan rings) Other e.g. FeS centres, Fe-haeme and Cu2+ Accepts Hs --> accepts electrons, which come from NADH
126
ETS: Poisons
Several poisons can react with molecules and blockage of ETC at any point prevents formation of ATP e.g. cyanide
127
Ubiquinone vs ubiquinol
Ubiquinone has 2 C=O bonds Ubiquinol replaces those carbonyl groups with two OH groups Changes conformation
128
Cytochrome C
Little protein with a haeme in it Unlike Q, carries e- one at a time Iron atom changes colour when reduced/oxidised Found in all aerobic organisms
129
NADH has a much higher ____ than FADH2
Driving capacity
130
The energy from fuel oxidation is converted to ATP by the process of...
Oxidative phosphorylation | But, this requires transfer of electrons to oxygen and the coupling of this power to synthesize ATP
131
Mitochondria and energy demands
The location and number of mitochondria is correlated with a tissue's energy demands
132
Complex I (NADH oxidase)
``` Works as a proton pump Pumps 4 protons per NADH Large L-shaped protein Contains FMN 7 FeS clusters ```
133
ΔG for NADH and FADH2
More negative for NADH
134
Iron-sulphur clusters
e- can effectively flow through these molecules as the Fe atoms can change oxidation state between Fe3+ and Fe2+
135
Complex I and II both...
Use Q10 | Converge on CIII
136
Complex III
Transfers 4 protons, 2x from reduced QH2, 2x from matrix by Q cycle Protons deposited on intermembrane space due to chemical reactions, NOT by pumps (technically transferred, not pumped)
137
Complex III: The complexity of the Q cycle is likely because...
Cytochrome C can only carry one e- at a time (aka cytochrome c oxidase) to CIV
138
Complex IV - overall
2 protons are pumped and the electrons flow to O2 to form H2O
139
Complex I - poisons
Blocked by some anesthetics and poison (rotenone) | Blocks binding point for ubiquinone
140
Complex III - poisons
Antimycin a - binds to CIII and disrupts e- flow and locks it down
141
Cytochrome C oxidase (CIV) - poisons
NO, H2S, CO and cyanide - bind to haeme groups --> stops oxygen flowing
142
Complexes I, III and IV transfer __ protons | Complexes II, III and IV transfer __ protons
10 protons | 6 protons
143
NADH moves ____ hydrogens than FADH2
4 more
144
What do flowing electrons power
Pumps and chemical transfer of H+ to form an electrochemical gradient (proton motive force / PMF), which is harnessed to drive ATP synthesis
145
What is the ATP synthase
A molecular machine Mirrors concept of water turbine of a hydrodam H+ flowing through the complex provide the force to push ADP and Pi tgt to form ATP
146
Complete oxidation of one molecule of glucose to six molecules of CO2 and H2O yields...
Approx 30-32 molecules of ATP
147
What is the most important regulator of oxidative phosphorylation
ADP
148
Net yield of oxidative phosphorylation - NADH and FADH2
~2.5 moles of ATP per mole of NADH oxidised | ~1.5 moles of ATP per mole of FADH2 oxidised
149
Overall, how much ATP does 1 glucose produce
28-38 | Variable
150
What is the bacterial rhodopsin?
A light-driven proton pump | Pumps protons into vesicle (inside out?)
151
What chemicals stop ATP synthesis
Chemicals that disrupt or 'uncouple' the proton gradient | Chemicals that poison electron flow
152
Proton motive force - components
``` 2 components in mitochondria; Conc gradient (ΔpH) and an electrical charge in mV ``` Both have an effect and can provide power --> electrochemical gradient Inside of mitochondria -vely charged, outside +vely charged
153
Where are ATP synthases located
All over ridges of cristae Appear to form lines Tightly arranged Proteins arranged in a V-shape for mitochondria
154
OXPHOS: How do protons flow?
Directly towards ATP synthases Since V-shaped, they shape the membrane and drag electrical charges on the phospholipids --> concentrated -ve charge around ATP synthases --> attracts protons --> localised conc of H+ --> low pH --> can turn ATP synthases = microdomain
155
ATP synthase - steps
1. H+ ions flowing down their gradient enter a half channel in a stator anchored in the membrane 2. H+ ions enter binding sites within a rotor (C-ring), making it click and changing shapes of each subunit so the rotor spins within the membrane 3. Each H+ makes one complete turn before leaving the rotor and passing through a second half channel in the stator into the mitochondrial matrix 4. Spinning of rotor causes an internal rod to spin, which extends like a stalk into the knob below it 5. Turning of rod activates catalytic sites in knob (held still by a stator) that produce ATP from ADP and Pi
156
Internal rod - shape and function
Not straight - slightly helical shape As it spins, it places forces against the alpha and beta F1 sub-units of catalytic region --> changes conformation This power is used to transform ADP and Pi to ATP
157
For each rotation of the internal rod...
3 ATP are made (because 3 sites) and protons drive the rotation
158
Helicases - function
As they move down, they... Split DNA Hydrolyse ATP Physically move strands of DNA Have 6 units working tgt - very similar to catalytic region
159
Catalytic knob sub-units
Effectively are a helicase working in reverse with the gamma sub-unit in the centre
160
NADH getting into mitochondria
Can't get into mitochondria by itself - two systems effectively transfer the electrons: - malate aspartate shuttle makes ~2.5 ATP - G3PDH shuttle makes ~1.5 ATP
161
Malate aspartate shuttle
Slow, complicated, but efficient
162
G3PDH shuttle
``` Less efficient (because FADH2, which means loss of ~1 ATP), but fast Multiple enzyme pathway ```
163
Summing up - 1 glucose
Net glycolysis makes 2 ATP and 2 NADH 2 x pyruvate --> acetyl-CoA makes 2x NADH 2 CAC makes 2 GTP/ATP, 6 NADH and 2 FADH2 OXPHOS converts 1 NADH --> ~2.5 ATP, or 1 FADH2 --> ~1.5 ATP
164
Why is the ATP yield (28-38) vague?
1. Temp - membranes leak H+ more when warm hot (less efficient), early expt done at only 25°C 2. NADH from glycolysis has 2 fates; malate aspartate shuttle or G3PDH shuttle 3. H+ are also used for other processes
165
Leigh's disease
Mutation in C-ring of ATP synthase Results in proton slippage Complex I appears to commonly fail / be impaired in disease states End up with aberration in brain
166
Damaged inner mitochondrial membranes - consequence
Increases leakiness to protons and structure changes | Consequences on ATP synthesis?
167
How can uncoupling ATP synthesis be useful
Makes heat As electrons flow through ETS, they make heat If flow faster through respiratory complexes, make more heat Protons pump faster Makes heat in lean people, obese people already have fat to keep them warm
168
K(M) and affinity
High Km = need lots of glucose = low affinity
169
NADH has ____
Energy | NAD+ can float through cell and carry energy from A to B (water soluble)
170
Nicotinamine
Oxidised form - has a positive charge | Can add electron, which is added with an H+
171
Glycolysis - substrate level phosphorylation
Capture ATP Phosphoglycerate kinase and pyruvate kinase Binds phosphate which has energy in it --> changes shape of enzyme --> grabs an ADP --> ATP
172
PFK - properties
Quite slow working Easy to turn on and off Amount of PFK is not huge - controls how fast the reaction goes
173
Two fates of glucose
Can feed into aerobic pathways | Can feed into anaerobic pathway - much less efficient but much faster
174
Anaerobic - no O2
Can't get rid of NADH at G3P
175
Pyruvate - acidity
Quite acidic
176
Production of lactate during anaerobic glycolysis
Lactate dehydrogenase - takes the Hs and passes it onto pyruvate that generates lactate NADH oxidised back to NAD and glycolysis can continue Lactate accumulates --> muscles hurt
177
Recycling of lactate
Still has energy in it, so is recycled through Cori cycle Exported into blood --> into liver --> turn lactate back into pyruvate --> turned back into glucose Process uses lots of ATP
178
CAC: Amino acids
Some amino acids can be fed directly into CAC
179
Where are CAC enzymes found
In matrix of mitochondria
180
Pyruvate breaks down into...
Acetate and CO2
181
Pyruvate structure
Has a carboxylate at the end --> removed to form CO2
182
Pyruvate dehydrogenase
A trifunctional enzyme (3 enzymes all arranged tgt)
183
Vitamin B1 (thiamine) - process
Pyruvate comes in with 3 Cs Thiamin diphosphate binds the acetate group and CO2 is removed Acetate binds to thiamine group --> passed onto lysine lipoamide (has S on end) Acetyl CoA (also contains a S) picks up the acetate, and lipoamide becomes reduced E3 containing FAD takes e- from lipoamide and becomes reduced --> FADH2 E3 donates extra e- to NAD --> NADH
184
FADH - reactivity
Quite reactive - always found bound within proteins (never floating around)
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What does the A stand for in acetyl-CoA
Acetate
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Acetyl CoA
Has sulfur and acetate in it | Acetate can be fed into CAC
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CAC - carbons
Cs get shuffled through the intermediates and some get pulled off as it goes Takes ~4 cycles for the C that's been injected to get spat out again as CO2
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α-KDH vs PDH
Very similar - similar ancestral origins Both poisoned by arsenic - binds to E2 and shuts it down Same process, but recognise diff substrates
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Succinate dehydrogenase (SDH) - process
Electrons flow to molecule Q Succinate comes in and a redox rxn takes place where a FAD is involved with dehydrogenation of C-H bonds Becomes a double bond (lose 2H) E- make their way down through Fe-S complex, and there is a heme where e- sit waiting Ubiquinone comes in and accepts e- and Hs
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FAD / FADH2 - structure
Have alloxan rings which can accept 2 Hs and thus carry e-
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CAC: Amphibolic - reactants and products
``` Acetyl-CoA --> ACh Citrate --> fatty acids α-ketoglutarate --> glutamate Succinate-CoA --> porphyrin (haemoglobin, cytochromes, chlorophyll) Malate -> glucose (gluconeogenesis) Oxaloacetate --> amino acid syntehsis ```
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Control of CAC - what slows down CAC
High ATP, acetyl-CoA, succinyl CoA and NADH | High NADH = lots of reducing power --> may drive unwanted rxns
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Pyruvate dehydrogenase (PDH) - regulation
Regulated allosterically Pyruvate, AMP, NAD, Ca2+ speeds it up Acetyl-CoA slows it down
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What does Ca2+ regulate
PDH, α-KDH and IDH When cells are polarised, Ca2+ floods in --> makes heart beat faster --> cell needs ATP --> turns enzymes on and makes them go faster
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Role of ETS
Take e- from NADH and FADH2 and transfer them through a series of e- carriers and other respiratory proteins/complexes Some move protons from matrix to IMS --> accumulate on one side --> chemiosmotic gradient Flows back through ATP synthase to make ATP
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ETS: Location of NADH and FADH
FADH situated lower, so packs less punch | NADH has a slightly higher potential (~1.135V) than FADH2 (~0.815V)
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ETS: Voltage
Voltage diff between top and bottom of ETS
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Complex I - where are the parts most likely from
Part in matrix likely from a primitive dehydrogenase | Part in membrane likely from ion pumps
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FMN vs NADH
FMN has greater reducing power --> can pull e- from NADH
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Complex I - cavities
To start with, cavities are facing down (into IMS) As charge is imparted, ubiquinone comes in and cavities open up to matrix Lining of these cavities have amino acids that attract protons Protons come into cavity and channel down
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ETS: Quinones
Can accept 2e- by binding 2Hs to form 2 OH groups Q10 = ubiquinone Q9 = ubiquinol Ubiquinone --accepts 1H--> semiquinone --accepts another H--> ubiquinol
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Complex II
Doesn't have power to pump, but does contribute to proton pumping overall Only part of CAC found in inner membrane FAD found within complex II (not floating around)
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Heme molecule
Iron atom surrounded by a porphyrin ring
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Which similar system is found in photosynthesis
Complex III
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How does rotenone work
Ubiquinone and rotenone have similar groups, so it can get into cleft and jams in there - irreversible
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Cytochromes
CII, III, IV and cytochrome c have metals bound within them Change colour as they are reduced/oxidised Mainly CIII, IV and cytochrome C
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If add rotenone, what happens to e- in ETS
Stops e- flowing at complex I --> run out of e- at end of chain Cytochromes / ETS becomes oxidised
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If add antimycin, what happens to e- in ETS
Poisons CIII End of ETS loses e- --> becomes oxidised Start of ETS (CI and Q) - accumulation of e- at CIII --> start becomes reduced
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If add cyanide, what happens to e- in ETS
Blocks CIV | E- stops at CIV --> builds up --> whole chain is reduced
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If hypoxia (low) or anoxia (no) oxygen, what happens to e- in ETS
E- builds up (can't bind with water) --> ETS reduction
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ETS: How many protons do the complexes pump
CI: 4 CIII: 4 CIV: 2 CII: 0
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NADH vs FADH - how many Hs do they move
NADH moves 4 more Hs than FADH (FADH less reducing power)
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Proton motive force - charge
Net -ve charge on inside of inner membrane of mitochondria Pushes equilibrium into more ordered state where we've generated a partition across the membrane As protons come back, they use the turbine to produce ATP
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pH difference across mitochondria
Not that large, and for ATP synthase to turn, needs a pH difference of 2 (quite large)
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Cristae work as...
A lightning conductor rod - focus electrical charges of protons towards the ATP synthase If proton flow is turned on, protons go through respiratory complexes - not randomly, but towards the ATP synthase
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Protons flowing through ATP synthases - steps
ATP synthases move into membrane Since V-shaped, they shape the membrane and drag electrical charges around the phospholipid --> concentrated -ve charge around ATP synthases --> attracts protons --> localised conc of protons --> very low pH at ATP synthases, which activates it Results in a microdomain near ATP synthases
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ATP synthase: Catalytic region is made from...
3 alpha and 3 beta subunits
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Brown adipose tissues
Uncoupling of ATP synthesis Allows protons to flow back through the protein Short circuits the ETS
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Cellular respiration: Adding succinate (substrate for CII)
Succinate provides e- that gets ETS to pump protons | MP increases
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Cellular respiration: Adding succinate then ADP and Pi
Addition of Pi drops MP a bit, but not all the way to baseline Still maintains a MP
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Cellular respiration: Adding succinate, ADP and Pi, then oligomycin (inhibitor of ATP synthase)
Oligomycin creates a block on ATP synthase ETS pumps a lot and starts to fill IMS with protons --> MP increases Decreases respiration rate
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Cellular respiration: Adding succinate, ADP and Pi, then dinitrophenol (DNP)
DNP allows respiration to accelerate and become maximal DNP drops ATP synthesis rates until zero because no more MP to drive ATP synthesis, and decreases pH gradient
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What is photosynthesis
The process of capturing and converging solar (electromagnetic) energy into chemical energy by plants, algae and bacteria
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Photosynthesis equation
6CO2 + 6H2O -->LIGHT--> C6H12O6 + 6O2
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Photosynthesis - What is reduced and what is oxidised
CO2 is reduced | H2O is oxidised - this is the only process in the whole of biology where water is oxidised
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Photosynthesis can be broken down into...
2 processes; 1. Light reactions 2. Calvin Cycle (dark reactions)
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Where does photosynthesis take place
Chloroplasts, mostly found in cells located just below the surface of the leaf
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Chloroplasts - structure
Highly organised internal structures | Contain pigments which can absorb visible light, generally referred to as chromophores
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Best known chromophore
Chlorophyll
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Chlorophyll - structure
Arranged in antennae within photosystems Perforin ring Long hydrophobic chain - keeps it embedded within photosystems Absorb light and become energised and resonate within PSs
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Photosystem names
PSII and PSI (in this order!)
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Photosynthesis: Light reactions - how is energy transferred between chlorophyll molecules
Via quantum tunnelling towards a special acceptor chlorophyll, which will lose an e- This e- is used to reduce a receptor molecule Light energy has become chemical energy
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Photosynthesis: Light reactions - what happens to the electron-deficient chlorophyll
It extracts an e- from another donor and cycle can be repeated
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Electron donors for PSI and PSII
Water is ultimate electron donor for PS2 | Plastocyanin (a special e- carrier) is e- donor for PSI
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Photosynthesis: Light reactions - equation
2H2O + 2NADP --> Light --> 2H+ + O2 + 2NADPH2 (+ ATP)
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Photosynthesis: Non-cyclic / linear photophosphorylation
The production of ATP and NADPH using the flow of e- from PSII to PSI
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Cyclic electron flow
Under certain conditions, photoexcited e- within PSI can take an alternative path called cyclic electron flow, which makes only ATP
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What is produced in light reactions that is used in the Calvin cycle
Calvin cycle uses NADPH and ATP from light reactions to fix CO2 from air to form G3P Consumption of ATP and NADPH by dark reactions is sustained by the light reactions
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Calvin cycle - input of light
Does not require direct input of light | But, do require products of light reactions; ATP and NADPH which are used in fixation of CO2 to produce sugars
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Calvin cycle - phases
Carbon fixation Reduction Regeneration of carrier (RBP)
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Calvin cycle - carrier
``` Ribulose bisphosphate (RuBP) CO2 is fixed to RuBP by enzyme ribulose bisphosphate carboxylase (RiBisCo) ```
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Product of Calvin cycle
A molecule of G3P, which requires input of 3CO2, 9ATP and 6NADPH
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How is glucose stored in plants
As starch and sucrose, which act as an energy source for plants
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Photorespiration
Where O2 competes with CO2 at RuBisCo | Undesirable for farmers
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Photorespiration - C4 plants
C4 plants have a solution to photorespiration and concentrate CO2 within adjoining cells within leaves This uses addition ATP which may come from cyclic e- flow
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Why does RuBisCo bind oxygen
While affinity for O2 is low, with intense light, photosynthesis can generate large amounts of O2, which is then incorporated into metabolites For plant, may eliminate harmful O2, thus C is not fixed and water is wasted
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How do C4 plants capture CO2
Using enzymes associated with other common pathways, e.g. phosphoenolpyruvate carboxylase
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C4 plants - Phosphoenolpyruvate carboxylase
Has a v high affinity for CO2, incorporates CO2 into a 4C intermediate in mesophyll cells where the Calvin cycle is less active C4 intermediates then pass into the bundle-sheath cells where CO2 is released to the Calvin cycle ATP required to drive this process, but chloroplasts of the bundle-sheath cells lack PSII, so all photosynthesis in this layer is cyclic, which makes addition ATP
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Main types of chlorophyll
Chlorophyll a and b
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Photoreceptive componds within the chloroplast are grouped tgt with other compounds to form...
Photosystems, and it is these complexes which absorb light
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Processes within photosystems are called the... and include...
Light reactions - splitting of water - NADP+ reduction - H+ gradient generation
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Thylakoid membrane - permeability
Impermeable to most ions and molecules, but not Mg2+ and Cl-
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Where do light reactions take place
Molecules in the thylakoid membrane
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Where do dark reactions (Calvin cycle) take place
Stroma
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Photosynthesis uses mostly _____ light
Blue and red i.e. these are the colours primarily absorbed and green is reflected Lack of absorbance at 500-600nm
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Excitation of isolated chlorophyll molecule
Electrons jump up to another orbital --> gain energy Comes back down and releases energy in two ways: - heat - gives off light at a shorter light, e.g. if hit by blue light, drops back down and gives a red fluorescnece
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Photosystem II structure
Chlorophyll molecules juxtaposed very closely tgt
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Photosystem II - process
Light hits PSII and makes its way to special chlorophylls (P680) As energy is imparted, e- jump up to special chlorophyll molecules that are missing Mg --> accepts e- and passes them onto quinones bound within PSII --> Pq Pq floats through cytochrome complex and unloads its protons and drags 2 protons from stroma into thylakoid space E- passed onto plastocyanin
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How a photosystem harvests light
Light strikes chlorophyll molecules and energy is transferred between them and gets trough special chlorophyll a molecule E- is excited and jumpts up into reaction centre That energy is then passed down through Pq then through a cytochrome complex which can contribute to ATP synthesis and e- passed to Pc
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Pq and Pc
Plastoquinone | Plastocyanin - has copper so blue in colour
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Chain of linear e- flow
PSII --cytochrome complex--> PSI
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Splitting of water and O2 release at O2 (e- holes)
Initial e- donor is chlorophyll molecules Protons knock e- out of orbits and form e-holes within atoms so must get e- There are 4 Mn atoms arranged tgt in PSII, which can grab water and rip protons from O and e- from within to fill holes of chlorophyll molecules Ultimate e- donor is water
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Photosystem I - process
Light hits PSI E- flow up to special acceptor molecules then to Fe-S complexes and reach ferrodoxin, which passes e- to NADP reductase E- are used by NADP reductase and passed onto NADP+ --> NADPH (e- carrier) - has reducing power Creates e- holes - Pc is carrying e-, which donates e- to fill the holes
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Where does photosystem I occur
Stroma
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Chloroplast ATPase (vs mitochondria ATPase)
Has 14 c-ring subunits compared to 8 in mitochondria - 6 more protons required to make ATPase turn than in mitochondria Are dimers in mitochondria
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Light reactions - there is a proton gradient developed by...
1. The splitting of water --> H+ released in thylakoid space | 2. Cytochrome complex transfers 4 H+ into thylakoid space
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Mitochondria vs chloroplasts - similarities
Have ETS Create gradient Make ATP through diffusion of H+ through ATPase
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Chloroplasts vs mitochondria - focal points
Chloroplasts don't have focal points to create a microdomain Mitochondria has MP that has electrical potential AND pH (conc of protons) Chloroplasts are permeable to Mg2+ and Cl- --> lose electrical potential --> must pump more protons into thylakoid space to generate gradient --> low pH - doen't need focal points since pH diff quite large
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Why are PSII and I separated
To do with cyclic electron flow
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What is cyclic electron flow
The other route of PSI
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Cyclic electron flow - process
Light hits chlorophyll (photon) E- jump up and pass down to PQ (not NADPH) which passes e- to Q cycle --> plastocyanin and feed back Fills its own holes Can generate proton gradient without splitting water
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Why is there structure in thylakoid membranes
Must separate linear and cyclic flow / pathways
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Why have cyclic electron flow
Produces ATP only (no NADPH) | C4 plants - require ATP
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Why is Calvin cycle confined to stroma
Stops intermediates and products being metabolised, as some intermediates feed directly into glycolysis Cell's normal pathway is full of glycolytic pathways so much keep separate or won't make sugar
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Calvin cycle: Phases - fixation
Done by RuBisCo 3x 5C molecules --> 3x 6C molecules (unstable) --> 6x 3C molecules Note: multiple molecules pass through the reactions so 6x ATP and NADPH
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RuBisCo
Most abundant protein Works / oxidised v slowly and v sensitive to changes in pH Highly concentrated in chloroplasts
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NADP vs NAD
As a rough rule, NADP/NADPH is involved in reducing reactions and NAD/NADH in oxidation reactions NADPH tends to be used for biosynthesis/regeneration
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Calvin cycle: Phases - reduction
Adds another phosphate and reduces it | Enzymes involved are phosphoglycerate kinase (takes ATP) and G3P dehydrogenase
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Calvin cycle: Phases - regeneration
After loss of 1x C3, 5x C3 are left | These are rearranged to 3x C5 and RuBP is regenerated
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Calvin cycle: To bind 3CO2...
Needs 6NADPH and 9ATP to give 6G3P (energetically expensive) One is removed to make sugar So 2 cycles required to make 1 glucose
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Calvin cycle: Only 1 G3P available for subsequent conversion to...
Half a hexose
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What is G3P
A simple triose sugar
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Regulation of Calvin cycle
pH - more alkaline stroma = faster Calvin cycle rate. stromal pH rises when light reactions are working Ferrethio reductase - needs NADPH to reduce/stabilise RuBisCo Explains why RuBisCo doesn't work well in isolation and needs light
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RuBisCo - issues?
Slow Makes a useless/toxic product (2-phosphoglycolate) and wastes water The faster it works, the more errors it makes (high temp increases rxn rate and error) When O2 si high (low CO2), up to 20-30% of photosynthesis is wasteful
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Evolution of a solution for photorespiration
``` Some plants (hot climates) can concentrate CO2 into oxaloacetate (4C plants) Partitioning of specific cycle into diff leave cells 4C oxaloacetate used as a CO2 shuttle ```
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C4 vs C3 plants
C4 have more spaces for gases Diff arrangement of cells and how they feed into each other, e.g. how water is delivered If temp high, stroma closes and regulates water loss and accumulates oxygen in leaves
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C4 vs C3 plants - photorespiration
C4 plants don't photorespire as much as C3 plants
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If C3 plants photosynthesise at a high rate...
O2 accumulates --> results in photorespiration - wasteful use of H2O and C already in CAC
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Since C4 system concentrates CO2...
It decreases photorespiration | C4 plants use more ATP, which comes from cyclic e- flow and sunlight is cheap
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When do C4 plants work more efficiently
Ultimately C4 plants use water more efficiently and function better in warmer climates
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Net reaction for glycogen synthesis
(glucose)n + glucose + 2UTP --> (glucose)n+1 + 2UDP + 2Pi
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Net reaction for glycogen breakdown
(glucose)n + Pi --> (glucose)n-1 + glucose-P
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Where is glycogen stored in most tissues
Cytosol
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Glycogen - solubility
Insoluble
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What is synthesis and breakdown of glycogen driven by
Synthesis driven by insulin | Breakdown driven by glucagon
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Which glycogen can release glucose to other tissues
Only glycogen in liver and a bit in kidney
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Mass of glycogen in liver and muscles
Liver can store 8-10% of wet mass as glycogen | Muscles can store 1-2% only - space limits in muscle
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Types of bonds in glycogen
α-1,4-glycosidic bonds | α-1,6-glycosidic bonds
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What is glycogen synthesis called
Glycogenesis
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Glycogenesis - process
Glucose goes through glucose transporter into hepatocyte but can equally go back, so must phosphorylate it to become G6P which is trapped by glucokinase in liver and hexokinase in muscle G6P becomes G1P to be committed to glycogenesis Pyrophosphorylase uses UTP UDP glucose now visible to glycogen synthase --> makes glycogen - grows long chain Gets to ~11 subunits long then a branching enzyme moves the sugars up 4 glycosyl units towards core and builds more to become more dense
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Glycogenesis - energy
Uses energy - endergonic
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Glycogenesis - where does the glycosyl group bind
The non-reducing ends, NOT the reducing end | α-1-4 glycosidic bonds and α 1-6 glycosidic bonds
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Branching of glycogen
Makes many termini = efficient storage and breakdown Created by transfer of ~7 glycosyl residues Each branch must grow to ~11 residues before transfer New branches are exactly 4 residues away and move in towards core
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What is glycogen breakdown called
Glycogenolysis
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Adrenaline drives glucose _____
Release If release is sustained, hypothalamus releases adrenocorticotropic hormone, which stimulates further release of adrenaline and cortisone --> enhances generation of glucose by liver and breakdown of glycogen
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Glycogenolysis - enzymes
Glycogen phosphorylase Glycogen de-branching enzyme (made of 2 enzymes) Phosphoglucomutase
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Glycogenolysis: Glycogen phosphorylase - energy requirement
Doesn't require ATP - uses Pi
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Glycogenolysis: Glycogen phosphorylase - process
Uses Pi in cytosol and adds to glucose molecule - not a hydrolysis, but breaks bond by phosphorolysis Forms G1P which is free into cytosol Works until we get to 5th glycosyl units leaving 4 left
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Glycogenolysis: Glycogen phosphorylase - why does it only reach the 5th glycosyl units
Due to steric hindrance - can't get all the way, but debranching enzyme can act as a transferase which transfers the 3 glycosyl units and leaves one, which is broken and hydrolysed (alpha-1,6) and glucose is free in cytosol Remaining glucose is trapped using an ATP and hexokinase
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Glycogenolysis: Glycogen phosphorylase - what is phosphoryolysis (not hydrolysis) important for
Hydrolysis will leave an un-phosphorylated glucose Ensures released glucose is charged and trapped in cells - important in muscles Saves an ATP each time - Pi is used directly, i.e. hexokinase isn't used
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Glycogenolysis: Phosphoglucomutase
Phosphate rearranged so G1P --> G6P Can be used for metabolism in cell Bypasses first step of glycolysis --> *glycolysis of G6P will yield 3ATP*
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Glycogenolysis: Glucose-6-phosphatase
Converts G6P to glucose, which can be used by blood and other tissues Only in liver and kidneys
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Coordinated control of glycogen metabolism
Stimulated/inhibited by glucagon or epinephrine (adrenaline) 2 cascades are activated by adrenaline - one switches glycogenolysis on, the other switches it off Ensures glycogen is not being made as it's being broke down
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Coordinated control of glycogen metabolism - cascade
A few molecules of adenylate kinase can make many molecules of cAMP (continuously for a while) which then interact with protein kinase A --> can have thousands which start to work on phosphorylase molecules and amplify the signal
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Glycogen storage diseases
11 known types Incidence ~2.5/100,000 births 7 result in muscle weakness or wastage 5 result in enlarged livers
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Von Gierke's disease (type I GSD)
G6Pase mutation or deficiency (can't release glucose from liver) Hypoglycaemia Excess G6P in liver shunted to triglycerides --> hyperlipidaemia (high levels of blood lipids / fats) Elevated lactate during fasting G6P can be shunted into diff pathways, one of them being pentose phosphate pathway, which can be converted into uric acid - forms crystal in joints - gout (hyperuricaemia) Enlarged liver and kidneys due to accumulated glycogen Treatment fructose and other carbs
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McArdle's disease
Glycogen in muscle but not released, but severe muscle cramps Lack of glucose release, little glycogen (myo)phosphorylase activity in muscle
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McArdle's disease: ADP level
Normal person: level of ADP doesn't change much from light exercise to heavy exercise McArdle's disease: dramatic increase in ADP with light exercise (inhibits lots of processes in cells, e.g. muscle cramps) - but if keep exercising and gain a second wind effect, ADP levels drop back down - shows the liver starts to release glucose but takes longer to occur
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McArdle's disease: what can also be used to support glycolysis / respiration
Proteins | Lipid by mitochondria, but not to same efficiency as glycolysis
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What is the word for 'to make glucose'
Gluconeogenesis
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Sources of building blocks for gluconeogenesis
``` Lactate --> pyruvate (Cori cycle) Amino acids (except leucine and lysine) Glycerol can be converted into glyceraldehyde and fed back up through gluconeogenic pathway (remainder of fats can't be used in animals to make glucose) TCA/CAC intermediates fed around and out mitochondria and into gluconeogenic pathway(conversion to citrate/oxaloacetate/malate) ```
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Cori cycle
Lactate is sent out to liver, which converts it back into glucose
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Where does gluconeogenesis occur
Only occurs in liver
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Overall gluconeogenesis equation
2pyruvate + 4ATP + 2GTP + 2NADH + 6H2O --> glucose 4ADP + 2GDP + 2NAD+ + 2H+ + 6Pi
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Gluconeogenesis - reversing glycolysis?
If glycolysis is simply reversed, ΔG is +ve | Using glyconeogenesis has -ve ΔG
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Gluconeogenesis - ATP usage?
Overall uses 11-12 ATP equivalents
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Gluconeogenesis - bypasses
``` 3 bypasses required for kinases as they don't reverse: Pyruvate kinase (bypass I) PFK (bypass II) Hexo/glucokinase (bypass III) ```
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Gluconeogenesis - Bypass I
Enzymes: pyruvate carboxylase, phosphoenolpyruvate carboxykinase (PEPCK) 2 ATP equivalents used NADH used = ~2.5-3 ATP NADH used at GAPDH - more ATP
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Gluconeogenesis - Bypass II
Enzyme: fructose 1,6-biphosphatase ATP is not reformed - the phosphate is lost
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Gluconeogenesis - Bypass III
Enzyme: glucose 6-phosphatase ATP is not reformed - the phosphate is lost
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Control of gluconeogenesis and glycolysis
Gluconeogenesis consumes ~12 ATP GLycolysis makes +2 ATP (or +3 from glycogen) --> mis-match of ~10 ATP Thus the 2 pathways must not run at the same time or net effect will be we burn lots of ATP Often will have opposite reaction from same metabolite on other side of pathway
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After 3 days of starvation, the brain’s energetic requirements are met by...
β-hydroxybutyrate Acetoacetate Limited glucose
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Why is anaerobic glycolysis very fast
Glycogen present in the cell can be rapidly mobilised Doesn't rely on O2 diffusion into cell Has fewer enzymatic steps than does the full oxidation of glucose to CO2 and H2O
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In absence of O2, glycolysis only proceeds if...
NADH can be oxidised and pyruvate is reduced
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The Cori cycle stores energy in the form of ____
Lactate
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What compound delivers ATP to hardworking muscles at the fastest and slowest rate
Fastest: Creatine phosphate Slowest: Stored fats oxidised to CO2
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Which enzyme occurs in the liver and permits glucose release to the blood
G6Pase
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Following intense exercise, blood lactate increases. This lactate is...
Oxidised by the heart and brain, or cleared through the liver by the Cori cycle
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What method did Melvin Calvin and Andrew Benson to resolve the Calvin cycle?
Paper chromatography with radioisotopes
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How many turns of the Calvin cycle is/are required to make a glucose molecule?
2
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Mitochondria vs chloroplast ATPase - number of subunits
ATPase of chloroplast has more subunits in its C-ring --> requires a greater proton gradient to drive ATP synthase
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Oxidised / reduced inorganic compounds can ultimately power life
Reduced
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H+ inhibits/stimulates glycolysis
Inhibits
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What process can C4 plants avoid
Photorespiration, but requires ATP
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Dinitrophenol
Acts as an ionophore | Dissipates the MP across the inner mitochondrial membrane
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The cytochrome complex of photosynthetic organisms shows strong similarities to which complex within mitochondria
Complex III
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It's hypothesised that e- move from each component of the Cyclic electron flow pathway in the following order...
Photosystem I --> ferredoxin --> cytochrome complex --> plastocyanin