biochemistry 2 Flashcards

You may prefer our related Brainscape-certified flashcards:
1
Q

where does the link reaction take place

A

mitochondrial matrix

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

what are the 3 stages of the link reaction

A

1) decarboxylation
2) oxidation
3) transfer to CoA

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

what causes arsenic poisoning

A

arsenic compounds react with sulfhydryl groups
- inactivates E2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

how is citrate used as an inhibitor

A

inhibitor of phosphofructokinase-1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

how is citrate converted into isocitrate

A
  • isomerisation by aconitase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

how is isocitrate converted into alpha-ketaglutarate

A
  • oxidative decarboxylation - removal of CO2
  • NAD+ to NADH
  • isocitrate dehydrogenase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

how is alpha-ketoglutarate converted into succinyl CoA

A
  • addition of CoA
  • CO2 removed
  • NAD+ to NADH
  • alpha-ketoglutarate dehydrogenase complex
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

how is succinyl CoA converted to succinate

A
  • succinate thiokinase
  • phosphorylation of either GDP to GTP or ADP to ATP
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

how is succinate converted into fumerate

A
  • oxidation - FAD to FADH2
  • succinate dehydrognase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

what does succinate dehydrogenase reduce

A

flavin adenine dinucleotides
(FAD)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

how is fumerate converted to malate

A
  • addition of H20
  • fumarate hydratase
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

how is malate converted into oxidate

A
  • malate dehydrogenase
  • NAD+ to NADH
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

what inhibits citrate synthesis

A

ATP and citrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

what inhibits and activates isocitrate dehydrogenase

A
  • inhibited by ATP
  • activated by ADP and NAD+
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

what inhibits alpha-ketoglutarate dehydrogenase complex

A
  • succinyl CoA
  • NADH
  • ATP
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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
Q

what is the outer mitochondria membrane permeable to

A
  • small molecules - <10kDa
26
Q

what is the inner mitochondrial membrane impermeable to

A
  • protons - has specialised special transport proteins
27
Q

where are respiratory chains found

A
  • inner membrane
  • 5 complexes
  • has adaptors of coenzyme Q and cytochrome C
28
Q

what is the function of respiratory chains

A
  • allows flow of electrons
  • generate a proton gradient
  • produces ATP from FADH2 and NADH
29
Q

what does complex I do

A
  • accepts electrons from NADH
  • passes these onto coenzyme Q
30
Q

what does complex II do

A
  • accepts electrons from FADH2
  • passes these onto conezyme Q
31
Q

what does complex III do

A
  • accepts electrons from coenzyme Q
  • passes these onto cytochrome C
32
Q

what does complex IV do

A
  • accepts electrons from cytochrome C
  • reduces oxygen to water
33
Q

what does complex V

A
  • protons pass through the channel
  • movement occurs
  • drives ATP synthesis
34
Q

what is complex V limited by

A
  • ADP concentration
35
Q

what are the inhibitors of the electron transport chain

A
  • cyanide
  • CO
  • rotenone
  • amytal
  • abtimycin
  • oligomycin
36
Q

where do inhibitors bind in the electron transport chain

A
  • binds to chain components
  • block electron transfer
37
Q

what does arginine react with and form

A

oxygen to from citruline and NO free radical

38
Q

what do scavenger reactive oxygen species do

A
  • protective enzymes
  • help neutralise reative oxygen speciles
39
Q

what does superoxide dismutase do

A

uses copper reactive centre to from intermediates - H2O2 and O2

40
Q

what does peroxidase catalyse do

A
  • uses a iron haem group to form intermediates - 2H2O and O2
41
Q

what do reactive oxygen species do and what are they used for

A
  • highly reactive and damaging
  • from pollution, smoke, radiation and drugs
  • used by phagocytes to kill cells
42
Q

what do ionophores do

A
  • activated by free fatty acids
  • transport protons from the cytosol to matrix
43
Q

what do uncouplers do

A
  • transport protons across the inner mitochondrial membrane into the matrix