biochemistry 2 Flashcards

1
Q

where does the link reaction take place

A

mitochondrial matrix

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2
Q

what are the 3 stages of the link reaction

A

1) decarboxylation
2) oxidation
3) transfer to CoA

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3
Q

what regulates the pyruvate dehydrogenase complex

A
  • phosphorylation inactivates E1 site
  • dephosphorylation activates E1 site
  • high energy charge decreases activity and low energy charge increases activity
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4
Q

what causes arsenic poisoning

A

arsenic compounds react with sulfhydryl groups
- inactivates E2

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5
Q

how is oxaloacetate converted into citrate and how is it regulated

A
  • additions of acetyl CoA
  • regulated by substrate availability
  • inhibited by citrate
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6
Q

how is citrate used as an inhibitor

A

inhibitor of phosphofructokinase-1

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7
Q

how is citrate converted into isocitrate

A
  • isomerisation by aconitase
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8
Q

how is isocitrate converted into alpha-ketaglutarate

A
  • oxidative decarboxylation - removal of CO2
  • NAD+ to NADH
  • isocitrate dehydrogenase
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9
Q

how is alpha-ketoglutarate converted into succinyl CoA

A
  • addition of CoA
  • CO2 removed
  • NAD+ to NADH
  • alpha-ketoglutarate dehydrogenase complex
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10
Q

how is succinyl CoA converted to succinate

A
  • succinate thiokinase
  • phosphorylation of either GDP to GTP or ADP to ATP
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11
Q

how is succinate converted into fumerate

A
  • oxidation - FAD to FADH2
  • succinate dehydrognase
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12
Q

what does succinate dehydrogenase reduce

A

flavin adenine dinucleotides
(FAD)

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13
Q

how is fumerate converted to malate

A
  • addition of H20
  • fumarate hydratase
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14
Q

how is malate converted into oxidate

A
  • malate dehydrogenase
  • NAD+ to NADH
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15
Q

what inhibits citrate synthesis

A

ATP and citrate

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16
Q

what inhibits and activates isocitrate dehydrogenase

A
  • inhibited by ATP
  • activated by ADP and NAD+
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17
Q

what inhibits alpha-ketoglutarate dehydrogenase complex

A
  • succinyl CoA
  • NADH
  • ATP
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18
Q

what is anaolerotic reactions

A
  • form intermediates to replenish other pathways
19
Q

what does fluroacetate inhibit and cause

A
  • inhibits aconitase
  • nausea, vomiting, abdominal pain, sweating, confusion, tachycardia
20
Q

what does arsenate inhibit and cause

A
  • inhibits alpha-ketoglutarate dehydrogenase complex
  • drowsiness, headaches, confusion, severe diarrhoea
21
Q

what does malonate inhibit and cause

A
  • inhibits succinate dehydrogenase
  • headaches, fatigue, poor appetite, sleeplessness, tremours, confusion, mapped chains, coma, death
22
Q

what does aluminium do to the TCA cycle

A
  • displaces iron
  • decreases activity of iron-dependent enzymes and oxidation sensitive enzyme activity
23
Q

what are the iron dependent enzymes

A

aconitase
succinate dehydrogenase
fumerase
complex IV - electron transport chain

24
Q

what are the oxidation sensitive enzymes

A

isocitrate dehydrogenase
alpha- ketoglutarate dehydrogenase

25
what is the outer mitochondria membrane permeable to
- small molecules - <10kDa
26
what is the inner mitochondrial membrane impermeable to
- protons - has specialised special transport proteins
27
where are respiratory chains found
- inner membrane - 5 complexes - has adaptors of coenzyme Q and cytochrome C
28
what is the function of respiratory chains
- allows flow of electrons - generate a proton gradient - produces ATP from FADH2 and NADH
29
what does complex I do
- accepts electrons from NADH - passes these onto coenzyme Q
30
what does complex II do
- accepts electrons from FADH2 - passes these onto conezyme Q
31
what does complex III do
- accepts electrons from coenzyme Q - passes these onto cytochrome C
32
what does complex IV do
- accepts electrons from cytochrome C - reduces oxygen to water
33
what does complex V
- protons pass through the channel - movement occurs - drives ATP synthesis
34
what is complex V limited by
- ADP concentration
35
what are the inhibitors of the electron transport chain
- cyanide - CO - rotenone - amytal - abtimycin - oligomycin
36
where do inhibitors bind in the electron transport chain
- binds to chain components - block electron transfer
37
what does arginine react with and form
oxygen to from citruline and NO free radical
38
what do scavenger reactive oxygen species do
- protective enzymes - help neutralise reative oxygen speciles
39
what does superoxide dismutase do
uses copper reactive centre to from intermediates - H2O2 and O2
40
what does peroxidase catalyse do
- uses a iron haem group to form intermediates - 2H2O and O2
41
what do reactive oxygen species do and what are they used for
- highly reactive and damaging - from pollution, smoke, radiation and drugs - used by phagocytes to kill cells
42
what do ionophores do
- activated by free fatty acids - transport protons from the cytosol to matrix
43
what do uncouplers do
- transport protons across the inner mitochondrial membrane into the matrix