Respiration Flashcards

1
Q

define substrate level phosphorylation

A

the formation of ATP via direct phosphorylation of ADP

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2
Q

when do you get substrate level phosphorylation? (3)

A
  • 1,3-Bisphosphate to 3-Phosphoglycerate
  • Phosphoenolpyruvate to Pyruvate
  • from GDP to GTP
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3
Q

Describe Structure of Mitochondria.

A

outer membrane
intermembrane space
inner membrane
matrix
cristae
mitochondria DNA
ribosomes
ATP synthase

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4
Q

DRAW OUT GLYCOLYSIS, LINK REACTION AND TCA WITH MAIN ENZYMES

A
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5
Q

Where does Glycolysis, Link Reaction, TCA cycle and Oxidative Phosphorylation Occur?

A

cytoplasm

3x Mitochondria

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6
Q

What is the NET ATP of Aerobic Respiration?

A

Glycolysis = 2ATP
TCA = 2ATP
ETC = 28ATP

= 32ATP

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7
Q

What is OIL RIG?

A

oxidation is loss of electrons
reduction is gain of electrons

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8
Q

What are the 3 Main Carriers?

A

ATP - Phosphate
NADH,NADPH,FADH2 - electrons and hydrogens
Acetly CoA - acetyl group

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9
Q

How is Energy Created under Anaerobic Conditions?

A

Fermentation of Yeast
- cannot do TCA or ETC
- pyruvate is produced but needs to be metabolised to balance NADH

= pyruvate - acetaldehyde - ethanol
= oxidation
- stops when too much ethanol created = toxic

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10
Q

What Happens if an Aerobic Respiration turns Anaerobic?

A
  • shortage of oxygen
  • TCA stops when it runs out of NAD and FAD
  • leads to lactic acid fermentation
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11
Q

Can other Sugars other than Glucose be Used?

A

Yes - galactose and fructose from adipose or liver

but efficiency is poor

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12
Q

What are the 4 Types of Regulation Mechanisms for Enzymes in Metabolism?

A

allosteric regulation
- enzyme activity can be inhibits

covalent modification
- phosphorylation

sequestration
- compartmentation or isolation of enzymes in specific parts of the cell

association with regulatory protein

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13
Q

How is Hexokinase Regulated?

A

allosteric regulation
- if there is too much glucose being converted to G-6P
- gets inhibits
- glucose stores as glycogen

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14
Q

How is Phosphofructokinase Regulated? (3)

A

allosteric reglation
- ATP binds to allosteric site and inhibits conversion of fructose-6-phopshate into fructose-1,6-bisphosphate

  • to increase affinity back up
  • PFK is activated by fructose-2,6-bisphosphate
  • reduces affinity to ATP
  • glycolysis continues
  • sensitivity to pH
  • if its too low, it reduces activity
  • prevents lactic acid formation
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15
Q

How is Pyruvate Kinase Regulated?

A

allosteric regulation and covalent modificaiton
- catalyse phosphophenolpyruvate into pyruvate
- activated by fructose-1,6-bisphosphate

too much energy, phosphorylates pyruvate kinase and makes it less active

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16
Q

How is Pyruvate Dehydrogenase Regulated?

A

allosteric regulation and covalent modificaiton
- convertes pyruvate to acetyl CoA

limiting sites
- limited by Acetyl CoA = E2 Transacetylase
- limited by NADH = E3 Dihydrolipodehydrogenase

  • phosphorylation switches off activity
17
Q

How is Isocitrate Dehydrogenase from TCA Regulated?

A
  • inhibited by ATP and NADH
  • activated by ADP
18
Q

How is a-Ketoglutarate Dehydrogenase from TCA Regulated?

A
  • inhibited by ATP, succinyl CoA and NADH
19
Q

What are the Main Enzymes in Glycolysis?

A

hexokinase
phosphofructokinase
pyruvate kinase
pyruvate dehydrogenase

20
Q

What are the Main Enzymes in TCA?

A

citrate synthase
isocitate dehydrogenase
a-ketoglutarate dehydrogenase

21
Q

what is isocitrate dehydrogenase, activated and inhibited by?

A

activated by ADP

inhibited by ATP and NADH

22
Q

what is a-ketoglutarate dehydrogenase inhibited by?

A

ATP, NADH, succinyl CoA

23
Q

What is the purpose of the ETC?

A

to reoxidise the co-enzymes used in glycolysis and TCA by transferring electrons

24
Q

Why cannot Electrons go Directly to the Electron Acceptors?

A
  • too much energy is released at once
25
Q

What happens at each Electron Transport Chain complex?

A

energy is used to push H+ across the inter membrane space, creating a gradient to the mitochondrial matrix

26
Q

Define Redox Potential, What Happens if the Value is Higher?

A

the measure of the tendency of a redox pair to lose a pair of electrons.

  • higher the positive value, higher the attraction to electron
27
Q

What is the Order of Electron Transporters and Why?

A
  • NADH-Q Reductase Complex
  • Succinate Dehydrogenase Complex
  • Cytochrome C Reductase Complex
  • Cytochrome C Oxidase Complex
  • increasing standard redox potential
28
Q

describe what happens in ETC

A

1) a FMN molecule accepts electrons from NADH = NAD+
- electrons pass through Fe-S complexes
===== 4 H+ into inner membrane space

2) succinate binds to a binding site bound to a FAD
- accepts electrons
- electrons pass through 3 Fe-S complexes
- FAD2-FAD

All electrons go to coenzyme q

3) transfer electrons from CoQ to cytochrome C
===== 4+ into inner membrane space

4) contains 2 copper centres and 2 haem groups
- 1st cytochrome c releases electrons and reduces 1st copper centre
- this in turn, reduces the 2nd copper centre

  • a 2nd cytochrome c releases electrons and reduces iron groups

== 2 reduced complexes
- iron binds to oxygen = peroxide iron
Fe-O-O
- a peroxide bridge forms between Fe-O-O-Cu

  • a 3rd cytochrome c release electrons and cleave O-O w/ H+
  • a 4th cytochrome c releases electrons and reduces Fe w/ H+

= oyxgen is the final electron acceptor
- uses 2 extra H+
- forms 2H20

29
Q

What is the Final Electron Acceptor?

A

oxygen