10.1-10.2 Step Zero of the Citric Acid Cycle Flashcards

(36 cards)

1
Q

What are two other names for the citric acid cycle?

A

Kreb’s or TCA cycle

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2
Q

Where does it take place?

A

Mitochondria

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3
Q

How much ATP is NADH worth?

A

2.5 ATP

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4
Q

How much ATP is FADH2 worth?

A

1.5 ATP

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5
Q

How much ATP is GTP worth?

A

1 ATP

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6
Q

When EC is low?

A

Pyruvate is metabolized by pyruvate dehydrogenase which forms acetyl-CoA and CO2

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7
Q

How is pyruvate transported in the mitochondria?

A

Transmembrane transporter protein

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8
Q

What does pyruvate dehydrogenase do?

A

Converts pyruvate to Acetyl CoA

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9
Q

What 5 coenzymes are needed?

A

NAD+/NADH
FAD/FADH2
CoA/CoAsh
TPP
a-lipoleic acid

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10
Q

NAD full name

A

nicotinamide adenine dinucleotide

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11
Q

FAD full name

A

Flavin adenine dinucleotide

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12
Q

CoA name

A

Coenzyme A

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13
Q

TPP name

A

Thiamine pyrophosphate

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14
Q

a-lipoleic acid name

A

Lipoamide

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15
Q

NAD characteristics

A

Derived from niacin (B3), involved in 200+ reactions, Transfers 2 electrons at once as hydride ion

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16
Q

Pellagra

A

niacin deficiency, rash/diarrhea/neurologic, fish veggies and poultry

17
Q

FAD characteristics

A

derived from riboflavin (B2), flavoproteins, a precursor to FAD and FMN.
Reduced to FADH2 by transfer of two electrons; one electron transported at a time; semiquinone intermediate

18
Q

Cheilosis

A

Riboflavin deficiency, swelled or cracked lips, almonds/meat/dairy, destroyed by light

19
Q

CoA characteristics

A

derived from pantothenic acid (B5), required for energy conversion in citrate cycle, cofactor in production of fatty aces, acetylcholine, heme, cholesterol.
Function - carry acetate in form of CoA

20
Q

Pantothenic acid deficiency

A

rare, found in most foods (chicken, yogurt, avocados)

21
Q

How do you get CoA across the membrane?

A

Nucleotide can’t cross; CoA degraded by enzymes into pantothenic acid, travels through circulation, crosses cell membrane, converted back to CoA with ATP and cysteine additon

22
Q

TPP characteristics

A

derived from thiamin (B1), absorbed in gut and phosphorylated, pulls acetyl group off pyruvate

23
Q

Beriberi

A

thiamin deficiency; anorexia/cardio problems/neurologic; brown rice and fortified grains - milling white rice removes bran and thiamin; raw fish and silkworms contain thiaminase which degrades thiamine

24
Q

ɑ-lipoic acid characteristics

A

Synthesized in plants & animals
– Also in broccoli, liver, spinach & tomato
* Provides reactive disulphide for redox rxns
* Receives acetyl from TPP and transfers it to CoA
The ball in the mechanism

25
Citrate Cycle Reaction 0
Substrates: pyruvate, NAD+, CoA Product: acetyl-CoA, NADH, COs, H+ Enzyme: Pyruvate dehydrogenase complex (E1, E2, E3) Irreversible
26
Reaction Zero for citric acid cycle
Pyruvate +CoA + NAD+ --> Acetyl CoA + CO2 +NADH +H+
27
Steps 1-3 of pyruvate dehydrogenase
1. E1 binds pyruvate, catalyzes decarboxylation → TPP intermediate & release CO2 2. TPP intermediate reacts with the disulfide of lipoamide group on E2 → lipoamide intermediate 3. E2 lipoamide intermediate carries acetyl group from E1 catalytic site to E2 catalytic site, reacts with CoA → acetyl-CoA & fully reduced dihydrolipoamide
28
Steps 4-5 of pyruvate dehydrogenase
4. Dihydrolipoamide group swings to E3, it’s reoxidized to a disulphide. A coupled rxn forms a dithiol on E3 then transiently forms E3-FADH2 5. The E3-FADH2 coenzyme intermediate is reoxidized in a coupled redox reaction producing NADH + H+
29
Ball and chain mechanism
E2 lipoamide picks up an acetyl group from E1 TPP
30
E2 can swing to bridge the gap
E2 ball and chain delivers acyl group to CoA in E2 catalytic domain
31
Oxidation
loss of electrons
32
Reduction
gain of electrons
33
Oxidant
compounds that oxidize other molecules – Accept electrons – Are reduced
34
Reductant
compounds that reduce other molecules – Donate electrons – Are oxidized
35
Reduction Potential (E)
Tendency for a molecule to gain electrons, driven by free energy (inverse relationship); favorable +E and -G
36
Using half-reactions to get ΔE
* Half-reactions can be used to determine change in reduction potential