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MBOD Block 4 > MBOD Block 4 Week 3 > Flashcards

MBOD Block 4 Week 3 Flashcards

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3
Q

Where are fats primarily stored?

A

In adipose tissue

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4
Q

How are fatta acids oxidized?

A

By B-oxidation pathway in mitochondria

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5
Q

What is the path of dietary fatty acids?

A

They are carried from the intestine to tissues to be metabolized as part of chylomicrons.

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6
Q

What is the path of stored fatty acids?

A

They are released from storage (lipolysis), and transported bound to serum albumin to be oxidized.

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7
Q

Which bond is cleaved in B-oxidation?

A

The alpha-beta bond.

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8
Q

What is Linolenate?

A

An 18 C FA with 3 double bonds (polyunsaturated); omega-3,6,9FA; Can also be called a cis delta-9,12,15 Octadecatrienoate.

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9
Q

Where do glucose and triglycerides from the diet or from the liver release go?

A

To make TG.

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10
Q

What are the stores of TG released as upon hormonal signals?

A

FA + Glycerol.

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11
Q

What do lipolytic hormones do?

A

Increases adipocyte cAMP and activation of lipase. Serum free fatty acid levels increase.

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12
Q

What are some lipolytic hormones?

A

Glucagon and Epinephrine

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13
Q

What is a antilipolytic hormone?

A

Decreases adipocyte cAMP. Decreased serum free fatty acid (FFA).

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14
Q

What is the major antyilipolytic hormone?

A

Insulin

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15
Q

What does a lack of insulin result in, esp in Type 1 diabetes?

A

Excessive lipolysis leading to ketoacidosis.

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16
Q

How do FA come into the muscle cell?

A

Carried on FA-albumin in the blood after the release by fat.

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17
Q

What are the activated transport intermediates in mitochondrial long-chain FA metabolism.

A

FACoA and FA carnitine

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18
Q

What are FACoA in the mitochondrial matrix oxidized to?

A

FAD2H, NADH, and AcCoA, which feed into the TCA and ETC or are made into Ketone bodies

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19
Q

How many carbons are in a short chain FA?

A

2-4

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20
Q

What type of membrane transport do short chain FA use?

A

Free diffusion

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21
Q

What type of membrane transport do medium chain FA use?

A

Diffusion

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22
Q

How many carbons are in a medium chain FA?

A

4-12

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23
Q

How many carbons are in a long chain FA?

A

12-20

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24
Q

What type of membrane transport do long chain FA use?

A

Carnitine cycle

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25
Q

What is the site of catabolism for very long chain FA?

A

Peroxisome

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26
Q

How many carbons are in a very long chain FA?

A

> 20

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27
Q

What are the metabolic routes for Fatty acyl CoA?

A

Energy, Membrane lipids, Storage

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28
Q

What is the role of Carnitine?

A

It carriers FA bound to it into the mitochondria.

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29
Q

What are the enzymes that reversibly transfer FACoA and FAcarnitine?

A

CPT1 and CPT2 (Carnitine palmitoyl-transferase I and II)

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30
Q

What facilitates the exchange of carnitine and acyl-carnitine?

A

Carnitine acylcarnitine Translocase

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31
Q

What is the first step of B-oxidation and the enzyme used?

A

Oxidize to double bond. Acyl CoA Dehydrogenase

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32
Q

What is the product of the first step of B-oxidation?

A

trans Fatty enoyl CoA

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33
Q

What is the second step of B-oxidation and the enzyme used?

A

Hydration adds -OH and -H across bond. Enoyl CoA hydratase

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34
Q

What is the product of the second step of B-oxidation?

A

L-B-Hydroxy acyl CoA

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35
Q

What is the third step of B-oxidation and the enzyme used?

A

Oxidize to double bond; C-OH=>C=O. B-hydroxy Acyl CoA Dehydrogenase

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36
Q

What is the product of the third step of B-oxidation?

A

B-Keto acyl CoA

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37
Q

What is the fourth step of B-oxidation and the enzyme used?

A

Cleaved (thiolysis). B-keto thiolase

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38
Q

What is the product of the fourth step of B-oxidation?

A

2 C shorter FACoA and AcCoA.

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39
Q

What are the similar processes between B-oxidation and the CAC?

A

Hydration, production of FADH2 and NADH

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40
Q

Where do the electrons from fatty acid oxidation go to; and what are the enzymes used?

A

The ETC. Acyl CoA dehydrogenase, Electron transferring flavoprotein (ETF), ETF-CoQ oxidoreductase.

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41
Q

How much does 1 palmitate undergoing 7 cycles of B-oxidation yield?

A

7 FADH2, 7NADH, 8AcCoA

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42
Q

How many ATP are produced by the 7FADH2 and 7 NADH?

A

28 ATP

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43
Q

How many ATP are produced by 8 AcCoA?

A

80 ATP

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44
Q

What is the net ATP yield from B-Oxidation?

A

106 ATP/palmitate

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45
Q

What is CPT1 inhibited by?

A

Malonyl CoA

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46
Q

What is the major control of FA oxidation?

A

Availability of FA

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47
Q

What occurs with oxidation of unsaturated FA?

A

The unconjugated double bonds are moved so that it becomes a conjugated double bond in the trans configuration.

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48
Q

What prevents double bonds from interferring with B-oxidation?

A

The isomerase and reductase working together.

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49
Q

What is the product of odd-chain FA oxidation?

A

Propinyl CoA and Acetyl CoA

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50
Q

What forms propionyl CoA?

A

The final thiolysis step in the oxidation of odd chain FA.

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51
Q

What are the two vitamins that are required for the metabolism of Propionic Acid?

A

Biotin and B12

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52
Q

What is the end product of the metabolism of Propionic Acid?

A

Succinyl CoA ->to CAC

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53
Q

What is Zellweger syndrome?

A

Lack of functional peroxisomes; defective import of proteins; VLCFA acumulate; liver kidney, and muscle damage.

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54
Q

What is formed from the oxidation of VLCFAs?

A

H2O2 and NADH

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55
Q

How long does the peroxisome oxidation of VLCFA repeat until?

A

Until there are 6-10 Carbons.

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56
Q

What is the result of Alpha-oxidation of branched chain FA?

A

PropCoA or AcCoA; repeats until the chain is 8C.

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57
Q

What does the branched chain FA that has been oxidized go to the mitochondria as?

A

FA-carnitine

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58
Q

What is Refsun’s Disease?

A

A rare neurological disorder caused by defective alpha-oxidation. Phytanic acid is deposited in nerve tissue.

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59
Q

What does omega-oxidation convert FA to?

A

Dicarboxylic acids

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60
Q

What is the fate of dicarboxylic acids after omega-oxidation?

A

They may be excreted or conjugated to glycine or carnitine.

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61
Q

What is the treatment for disorders of FA Oxidation?

A

Avoid fasting; more smaller meals; less fat; provide energy needs with carbs-controls lipolysis and decreases dependence on fats and ketones for energy.

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62
Q

What does the B-oxidation of “even chain” FA in the mitohondria produce?

A

AcCoA, FADH2, and NADH

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63
Q

What does the B-oxidation of “odd chain” FA in the mitohondria produce?

A

FADH2, NADH, AcCoA, and propionyl CoA ->succinyl CoA

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64
Q

What does the B-oxidation of unsaturated FA in the mitohondria require?

A

Two extra enzymes, an isomerase and a reductase to modify the double bonds.

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65
Q

What do peroxisomes specialize in?

A

Very long and long-chain fatty acids (n>8).

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66
Q

What do peroxisomes produce?

A

AcCoA, FADH2, and H2O2.

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67
Q

What are branched-chain phytanic acids oxidized by?

A

Alpha-oxidation

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68
Q

What does alpha-oxidation do?

A

It removes one carbon from the carboxyl end.

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69
Q

What does B-oxidation alternately release in peroxisomes when dealing with branched-chain phytanic acids?

A

AcCoA and Propionyl CoA until the chain reaches 8 C, then it leaves the peroxisome as fatty acyl-carnitine.

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70
Q

Where does omega-oxidation occur?

A

In the ER.

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71
Q

What can accumulate abnormally in omega oxidation if B-oxidation is defective?

A

Dicarboxylic acids

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73
Q

What is the main thing that is occuring in the Fed State?

A

Glucose, FA, AA is used for fuel or stored.

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74
Q

What is the main thing that is occuring in the Fasted State?

A

Fat starts breaking down TG to FA and glycerol

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75
Q

What is the main thing that is occuring in the Basal Fasted State?

A

Fat releases FA which is used for energy and Ketone Body synthesis.

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76
Q

What is the main fuel source in the Starved State?

A

FA

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77
Q

Whatbecomes fuel for the brain in the Starved State?

A

KB

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78
Q

What are the key fuels in the fasting state?

A

Ketones

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79
Q

Where is HMG CoA synthase found?

A

In liver mitochondria

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80
Q

Where are ketones only made?

A

In the liver

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81
Q

What are the ketone bodies made in liver and metabolized in muscle, brain, etc.

A

Acetoacetate and B-hydroxybutyrate

82
Q

What can acetoacetate be spontaneously decarboxylated to?

A

Acetone

83
Q

What is the first step in ketone synthesis?

A

Two acetyl CoA condense to produce Acetoacetyl CoA.

84
Q

What is the condensation of 2 Acetyl CoA catalyzed by?

A

Thiolase

85
Q

What is the second step in ketone synthesis?

A

Acetoacetyl CoA and Acetyl CoA form HMG CoA

86
Q

What catalyzes the formation of HMG CoA in ketone synthesis?

A

HMG CoA synthase

87
Q

T/F The Liver can use ketones.

A

False

88
Q

What is the third step in ketone synthesis?

A

HMG CoA is cleaved by HMG CoA lyase to form acetyl CoA and Acetoacetate.

89
Q

What can acetoacetate be reduced to and by what enzyme?

A

B-Hydroxybutyrate; by B-hydroxybutyrate dehydrogenase. (reversible reaction)

90
Q

How is acetone excreted?

A

Via the lungs

91
Q

How can acetone be detected in the body?

A

By its odor - ketone breath

92
Q

When can ketones partially replace glucose as fuel?

A

During fasting and starvation

93
Q

What can acetoacetate and B-hydroxybutyrate affect in the body?

A

They can affect pH (ketoacidosis) and enter the urine (ketonuria), and cause extreme ketone body concentration (Ketosis). Can cause coma and death.

94
Q

What is the key factor in the control of ketone synthesis?

A

Availability of FA

95
Q

How is ketone synthesis regulated?

A

High NADH depletes OAA to help shunt AcCoA to make ketone bodies because less OAA is available for citrate.

97
Q

What are the steps during pyruvate oxidation where NADH is produced?

A

Pyruvate dehydrogenase; isocitrate dehydrogenase; alpha-ketoglutarate dehydrogenase; malate dehydrogenase

98
Q

What is the step in pyruvate oxidation where FADH2 is formed?

A

Succinate dehydrogenase

99
Q

What do NADH and FADH2 give up to the ETC?

A

Their protons and electrons.

100
Q

What creates a gradient across the mitochondrial inner membrane?

A

The pumping of protons by the protein complexes.

101
Q

What is used as a source of energy to generate ATP by the ATP synthase?

A

The proton gradient.

102
Q

What is the final step in the electron transport process?

A

Export of the newly formed ATP out of the mitochondrion to the cytosol where it can be used for synthesis, transport, etc.

103
Q

When electrons move spontaneously between two compounds, which direction do they move?

A

In the direction that releases free energy.

104
Q

Where do the electrons in NADH and FADH2 have a tendency to move?

A

To more positive reduction potentials and release free energy as they move.

105
Q

How is the free energy of the electrons conserved in a chemical and electrical gradient?

A

By pumping the protons out of the matrix across the inner membrane.

106
Q

What is Complex I of the ETC?

A

NADH Dehydrogenase complex

107
Q

What are the two domains that complex I is composed of?

A

The membrane arm and the peripheral arm.

108
Q

What does the peripheral arm of Complex I contain?

A

Most of the redox active centers.

109
Q

What does the membrane arm of complex I contain?

A

All of the mitochondrially encoded subunits.

110
Q

What is the inhibitor of complex I?

A

Rotenone

111
Q

How does Rotenone inhibit complex I?

A

It binds to complex I and competes at one of the ubiquinone binding sites. Electron transfer from complex I is blocked.

112
Q

What is the stoichiometry of protons pumped to electrons transferred?

A

4 protons to 2 electrons

113
Q

How many electrons are passed for each NADH oxidized?

A

two

114
Q

What are the three subunits in the membrane domain of complex I?

A

NuoM, NuoN, and NuoL; proton translocating subunits.

115
Q

How many protons per pair of electrons does complex I pump?

A

Four

116
Q

What are iron-sulfur centers?

A

Redox active ceners that can accept and then donate electrons in the electron transfer pathway.

117
Q

What are the different varieties of the iron-sulfur clusters?

A

2Fe-2S; 4Fe-4S cluster; a 1Fe center coordinated with four cysteines; 3Fe-4S cluster

118
Q

What do iron-sulfur clusters act as a conduit for?

A

For the electrons to travel from the FMN to ubiquinone.

119
Q

What is FMN?

A

A cofactor tightly bound to the peripheral arm of complex I. (Flavin mononucleotide)

120
Q

What are the four flavoproteins that feed electrons to ubiquinone?

A

Complex I, Complex II, Electron transfer flavoprotein dehydrogenase, sn-glycerophosphate dehydrogenase (an NADH shuttle)

121
Q

What is the common thing among the flavoproteins?

A

The flavin gets the electrons first and then passes them on to the iron-sulfur centers.

122
Q

What is the role of NADH in the ETC?

A

It is an obligatory 2 electron donor.

123
Q

What is the role of Fe3+ in the ETC?

A

It is an obligatory one electron acceptor.

124
Q

What is complex II?

A

A tetramer of non-identical subunits. It contains FAD and three iron sulfur clusters.

125
Q

What is the only TCA cycle enzyme that is an integral membrane protein.

A

Succinate dehydrogenase

126
Q

What does complex II consist of?

A

A tetramer of non-identical subunits. It contains FAD and three iron sulfur clusters. Two small hydrophobic membrane subunits with a heme sandwiched between the subunits.

127
Q

What flavoprotein is part of the glycerophosphate shuttle for moving electrons from cytosolic NADH inot the electron transfer pathway?

A

Sn-glycerophosphate dehydrogenase.

128
Q

What reaction does glycerophosphate dehydrogenase perform?

A

It converts dihydroxyacetone phosphate (DHAP) to glycerol-3-phosphate.

129
Q

In which cells are levels of the mitochondrial form of the glycerol 3-phosphate dehydrogenase high?

A

Pancreatic islet cells.

130
Q

What protein might be a candidate gene involved in patients with non-insulin dependent diabetes mellitus (NIDDM)?

A

Glycerol 3-phosphate dehydrogenase (levels are low)

131
Q

What is ubiquinone?

A

A lipid soluble electron carrier that carries electrons between complexes in the electron transport pathway.

132
Q

How many electrons can ubiquinone accept at a time?

A

One

133
Q

What is ubiquinone called when it has accepted only one electron?

A

A semiquinone.

134
Q

What is the state of ubiquinone when it has two electrons?

A

It is fully reduced.

135
Q

What is the state of ubiquinone when it has no electrons?

A

It is fully oxidized.

136
Q

How os the semiquinone stabilized?

A

By binding to protein sites.

137
Q

What is another name for complex III?

A

The bc1 complex.

138
Q

What are the extra subunits of complex III called that have no known function?

A

Supernumerary subunits.

139
Q

What are the redox centers that you must know to understand complex III?

A

Two b type hemes that are contained in the same subunit and are directly above one another in the membrane and perpendicular to the membrane.

140
Q

What is the mechanism that complex III operates by?

A

The Q cycle.

141
Q

Where does the ubiquinone become oxidized?

A

At center P or the oxidation center.

142
Q

What two paths are the two electrons of ubiquinone split into?

A

The Rieske iron sulfur center and the first b heme called BL.

143
Q

Which path would the electrons prefer to choose?

A

The pathway toward the most positive reduction potential - to the iron-sulfur center.

144
Q

What is the structure that forces the splitting of the electrons?

A

The bc1 complex.

145
Q

What is the path of the electron that goes from the iron-sulfur center?

A

It goes to cytochrome c1 and is finally passed on to cytochrome c; it is used to reduce oxygen in complex IV, cytochrome c oxidase.

146
Q

What is the path of the other non-productive electron from the first b heme BL?

A

It passes on to the second b heme BH and is given to a fully oxidized ubiquinone at the N center or reduction center.

147
Q

What is the net movement of protons for every two ubiquinones that get oxidized?

A

4 out at the cytosol and two in from the matrix

148
Q

How does Antimycin act as an inhibitor to complex III/bc1 complex?

A

It binds very tightly to the N center at the matrix side of the membrane and prevents electrons from reaching unbiquinone from the b hemes.

149
Q

What binds at the P center and prevents entry of the loosely bound ubiquinone and stops electron flow through the complex?

A

Stigmatellin

150
Q

How many electrons does it take to reduce oxygen?

A

4

151
Q

What is charge compensation?

A

To take up a proton to compensate for the cost of using a electron. May be part of the driving force for proton pumping.

152
Q

What are the redox centers in cytochrome c oxidase?

A

Copper A and copper B.

153
Q

What are the contents of Copper A?

A

Two coper ions near one another; two hemes of the a type-heme a and heme a3; a magnesium ion and a zinc ion.

154
Q

Where is the first place the electron goes upon leaving cytochrome c?

A

The copper A site.

155
Q

What forms the binuclear center in cytochrome c?

A

Heme a3 and copper B

156
Q

What forms a supercomplex?

A

Complex I, a dimer of complex II and complex IV.

157
Q

What does the supercomplex facilitate?

A

It allows efficient transfer of electrons down the pathway.

159
Q

What is ATP synthase?

A

A molecular motor that synthesizes ATP using the energy stored in the proton and membrane potential gradient.

160
Q

What does the F1 part of ATPase contain?

A

The catalytic subunits

161
Q

What does the Fo part of ATPase contain?

A

The proton channel; the stalk and 10 c subunits.

162
Q

What happens when ATP synthesis is said to be uncoupled from respiration?

A

The F1 part of the ATPase is removed from the membranes; the oxidative phosphorylation cannot work.

163
Q

What are the ways that mitochondria can become uncoupled?

A

Their membranes can be leaky; the addition of a chemical uncoupler

164
Q

What are the chemical uncouplers?

A

Serve as one-way proton carriers what shuttle a proton across the membrane down the gradient. Include CCCP, 2,4-dinitrophenol (DNP), FCCP.

165
Q

What is state 3 respiration?

A

Rapid oxygen consumption.

166
Q

What is state 4 respiration?

A

When the ADP runs out and the slope drops back to a much lower level.

167
Q

What is the appearance of the mitochondria when they are in state 3 respiration?

A

They have a large periplasmic space and the matrix appears condensed.

168
Q

What is the appearance of the mitochondria when they are in state 4 respiration?

A

More typical with very little periplasmic space.

169
Q

What is the uncoupler protein?

A

UCP1; termogenin; transports fatty acid anions across the inner membrane from the matrix in exchange for a counter ion.

170
Q

What is the uncoupler protein activated by?

A

Free fatty acids that are produced by lipolysis in response to hormones.

171
Q

What is a required cofactor of uncoupling protein?

A

Ubiquinone

172
Q

What is the chemiosmotic hypothesis?

A

The inner membrane is impermeable to protons, which permits the controlled leak of protons down the gradient through the ATP synthase to make ATP.

173
Q

What happened when light was applied to bacteriorhodopsin in a reconstitution experiment?

A

They pumped protons into the vesicles; the ATP synthase was able to make ATP.

174
Q

What does the c subunit of the Fo subunits have in the middle of the helix?

A

Aspartate, which is required for the proton channel.

175
Q

What is required for the F1 particle to be sensitive to oligomycin?

A

OSCP-oligomycin sensitivity conferring protein.

176
Q

What is an antibiotic inhibitor of the ATPase?

A

Oligomycin

177
Q

What is the subunit composition of F1?

A

Alpha 3, beta 3, gamma, delta, epsilon.

178
Q

Which subunits of F1 are the active catalytic subunits?

A

The beta subunits

179
Q

What causes distortions or conformational changes in the beta subunits of F1?

A

The significant differences in the gamma subunit interactions with the three catalytic beta subunits.

180
Q

What is the model of how the ATP synthase works called?

A

The binding change mechanism.

181
Q

What is the first postulate of the binding change mechanism?

A

That the energy of the proton gradient is not used to form ATP but to release ATP from a very tight binding site where it forms spontaneously.

182
Q

What does the release of tightly bound ATP require?

A

The energy of the proton gradient converted into the mechanical energy of protein conformational changes.

183
Q

What is the second postulate of the binding change mechanism?

A

That the three catalytic sites are each in a unique conformation and the conformations are interconvertible.

184
Q

What are the three catalytic sites that represent the different stages of the catalytic cycle?

A

L-loose; T-tight; O-open

185
Q

What is the third postulate of the binding change mechanism?

A

That conformational changes at the three sites are driven by rotation of the asymmetric gamma subunit relative to the F1 ball.

186
Q

T/F Energy is needed to release ATP

A

True

187
Q

What is the P/O ratio?

A

How many ATP molecules are produces per oxygen consumed.

188
Q

How many electrons and protons does it take to reduce oxygen to water?

A

4

189
Q

What is the elevator model?

A

It suggests that protons start their passage through the membrane in subunit a, then move onto one of the c subunits which then carries the proton as the ATPase rotor moves 1/12th or 1/10th of a full circle.

190
Q

T/F The number of c subunits dictates efficiency.

A

True

191
Q

How many ATP are produced per 4 protons?

A

One

192
Q

What subunits form the rotor of the molecular motor of ATP synthase?

A

The c subunit ring is attached to the epsilon and gamma subunits.

193
Q

What subunits form the stator of the stationary part of ATP synthase?

A

a subunit, b subunit, apha, beta and delta subunits.

194
Q

How many ATP do we get for one glucose?

A

32 ATP

195
Q

How many times per day does the ATP in your body turn over?

A

About 200 times.

196
Q

What is the flux of adenine nucleotide through the ADP/ATP carrier close to every day?

A

Your body weight.

198
Q

What are the two roles of cytochrome P450?

A

Drug metabolism and Lipid metabolism

199
Q

Where did cytochrome P450 get its name from?

A

P=pigment, strong absorption band at 450nm; a reduced CO difference spectrum; proteins have a heme group.

200
Q

What ligand is above the plane of the heme in cytochrome P450?

A

Thiolate anion, a sulfur with a negative charge.

MBOD Block 4 (5 decks)

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