6a Flashcards

1
Q

where does the krebs cycle // citric acid cycle occur and what does it do

A

it occurs in the mitochondria

its the aerobic oxidation of pyruvate

or the oxidation of all fuels such as lipids, amino acids and sugars.

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2
Q

Krebs cycle: oxidation of fuels!! what form do fuels enter the krebs cycle in

A

they enter the cycle as acetyl coenzyme A

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3
Q

end product of glycolysis is

A

pyruvate

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4
Q

what comes after glycolysis

A

krebs cycle

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5
Q

whats the starting material of the krebs cycle

A

the starting material is acetyl coenzyme A

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6
Q

where does glycolysis occur in

A

the cyctoplasm

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7
Q

does glycolysis produce a lot of ATP

A

nope!!

u only get 2ATP and 2 pyruvate from 1 glucose molecule.

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8
Q

for glycolysis to occur,, what needs to keeo happening

A

NAD+ needs to keep being regenerated or else the cycle stops!!

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9
Q

what processes regenerate NAD+

A

fermentation and the lactic acid cycle regenerate NAD+

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10
Q

what part of acetyl coenzyme A do we need to remember,, the lhs but describe it

A

Me carbonyl S, C C NH carbonyl

thats the structure we care about.

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11
Q

whats an acetyl group

A

an acetyl group is the carbonyl group with an Me as one of the R groups.

looks like acetone kinda ig

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12
Q

okay so if acetyl coenzyme A has 2 important acetyl groups in the part we are about,, and its the starting material of the krebs cycle,, what does the krebs cycle do to the 2 acetyl groups

A

it oxidises the 2 acetyl groups into CO2!!

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13
Q

from glucose,, glycolysis to the krebs cycle, what happens to all of the carbons

A

the. arbons are converted into CO2 in a series of step wise reactions,, these reactions give out energy in small amounts.

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14
Q

describe the cycle of the krebs // citric aiid cycle

A

start // top = acetyl coenzyme A

  • 2CO2 (oxidation of the 2 acetyl groups)
  • 8e- (from the NADH and FADH)
  • 1GTP

back the the beginning

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15
Q

what happens after the krebs cycle // cirtric acid cycle

A

oxidative phosphorylation!!

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16
Q

what links the krebs sycle and oxidative phosphorylation + what happens in it

A

the 8e- we get from NADH and FADH (the e- come from the H)

they’re given out during the krebs cycle and enter oxidative phosphorylation.

where they enter the electron transport chain and reduce 2O2 to give 4H20

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17
Q

okay so the 8e- enter oxudative phosphorylation and reduce 2O2 to give 4H20,, what else happens in oxidative phosphorylation and what powers this

A

ADP + Pi —> ATP.
atp synthesis is here!!! this is the reaction where most our ATP is regenerated from.

this ATP synthesis is powered due to the H+ gradient,, aka proton gradient which gets pumped in.

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18
Q

what regenerates NAD+ from NADH

A

fermentation, lactic acid fermentation

and the reduction of 2O2 into 4H20!! bc the e- we use to reduce come from the H’s in NADH and FADH!!! so yhhh

19
Q

how do we convert pyruvate to acetyl coenzyme A

A
  • decarboxylation
  • oxidation
  • pyruvate + coenzyme A(long chain thiol) + NAD+
    — pyruvate dehydrogenase—> acetyl coenzyme A + CO2 + NADH + H+
20
Q

going from pyruvate to acetyl coenzyme A,, what enzyme do we use

A

we use pyruvate dehydrogenase

21
Q

pyruvate dehydrogenase exp

A

3 distinct enzymes:

  • pyruvate dehydrogenase: TPP: oxidative carboxylation (-CO2 from pyruvate by attaching it to the NS nucleophilic heterocycle)
  • dihydrolipoyl transcetylase: lipoamide: acetyl transfer
  • dihydrolipoyl dehydrogenase: FAD: regenerates lipoamide!!!
22
Q

describe the mechanism of pyruvate decarboxylation

A

the NS heterocycle has an acidic H between the N and S.

this is removed and forms a (-),, this attack the keto bit of pyruvate as its more electrophilic than the ester bit.

decarboxylation then occurs as the OH e- go to the C-O bond to form CO2. which then kicks itself off the molecule,, gives the bigger molecule a C=C enol double bond,, and then neutralises (+) nitrogen

23
Q

enol carbons are normally what

A

theyre normally nucleophilic as the O,, or any other heteratoms can use their lone pairs to resonate their lone pairs towards it,, allowing the C=C to attack an electrophile.

24
Q

describe pyruvate dehydrogenase and lipoamide (E2)

A

we have the lipoamide which is the S-S heteroamide

the S-S is electrophilic and can therefore be attacked by a nucleophile such as the NCS heterocycle with the anion on the C.

when this ttacks the S-S it opens the ring

deprotonation then occurs to kick the NCS ring off the lipoamide to form an acetyl protected thiol. bc theres 2 acetyles on both ends and thiols in between.

25
whats the NCS anionic ring
its a thiazonium ion which is regenerated after attacking the lipoamide.
26
describe dihydrolipoyl transferase and coA (E2)
the acetyl protected thiol is reacted with coenzyme A to give acetyl coenzyme A and a dihydrolipoamide the coenzyme A displaces the lipoamide (addition elimination) coenzyme is added to the acetyl (the thioester - bc its more eletrophilic due to diffuse orbitals overlapping with the CO* orbital - and kicks off the lipoamide bit,, giving u acetyl coenzyme A and the dihydrolipoamide.
27
once we form the acetylcoenzyme A and dihydrolipoamide what do we need to do
we need to oxidise the dihydrolipoamide to get the electrophilic S-S heterocycle back in order to use it in reactions. this is done by reducing FAD into FADH2 and using an enzyme with a disulphur bridge on it. ur basically forming another disulphide bridge between the enzyme and dihydrolipoamide,, then reforming the SS heterocycle. the SS heterocycle is called a lipoamide!!!!!! type thing. but only one side of the lipoamide.
28
why is the thioester more reactive than the OH ester.
bc S is a larger atom,, meaning its orbitals are larger and therefore more diffuse. this means that they have poorer overlap and therefore less efficient overlap between the CO* and itself. therefore the C is more electrophilic in the thioester than the oxygen ester. the thiol is also a better LG for the addition elimination with Coenzyme A due to being more polarisable and therefore having a lower entropy loss when u hydrate the ion.
29
complete citrci acid cycle equation:
acetyl coA + 3NAD+ + FAD + GDP + Pi + 2H2O ---> 2CO2 + 3NADH + FADH2 + GTP + CoA + 2H+.
30
what happens to acetylcoenzyme A once weve made it
it reacts with oxaloacetate to form citrate!!
31
is the oxaloacetate the electrophile or nucleophile is the acetyl coenzyme the electrophile or nucleophile
oxaloacetate is the electrophile as it has a carbonyl the acetyl coenzyme also has a carbon but it has enolisable alpha protons which can be removed to give an enolate. which acts as a nucleophile and attacks the oxaloacetated
32
describe citrate synthesis: u have oxaloacetate and acetyl coenzyme A
acetyl coenzyme forms an enolate and attacks the electrophilic carbonyl on oxaloacetate. water then attacks the leftover carbonyl on acetyl coenzyme A and the carbonyl forms an OH. the water that was added obvs turns into an OH,, which is then deprotonated to give a new carbonyl and kick of the CoA. which is a good leaving group bc its a thiol meaning it can stabilise the negative charge well and its easily enolisable.
33
whats important about citrate synthesis : acetyl coenzyme A and oxaloacetate
oxaloacetate must bind to the enzyme first in order to change its conformation this change in conformation creates the acetyl coenzyme binding site. this is important to prevent undesired hydrolysis of acetyl coenzyme A.
34
before the hydrolysis of acetyl coenzymeA in the synthesis of citrate,, what must happen
aldol reaction between the acetyl coenzyme A nucleophile and the electrophilic carbonyl of oxaloacetate. thennnnn hydrolysis of acetyl coenzyme A!!! not before. this is why the induced fit is important bc it prevents the acetyl coenzyme fitting the binding site before the aldol reaction happening.
35
what does citrate form
it forms isocitrate
36
whats the difference between isocitrate and citrate
citrate has an OH on the 3rd carbon,, isocitrate is an isomer of citrate as the OH is moved to the first carbon
37
how is isocitrate formed from citrate
aconitase enzyme performs the isomerisation it catalysed the dehydration (-H2O) and then the 1-4 addition of H2O onto the 2nd Carbon.
38
when making isocitrate from citrate,, is H2O added on the back face or front face
the back face!!! so its o the Re face!!!!
39
what reaction aka sn1, sn2 etc happens to get from citrate to isocitrate
the E1CB reaction bc OH is a bad LG but it has to gooooo.
40
what happens to isocitrate
isocitrate undergoes decarboxylation then oxidises the OH to form a ketone... to form alpha ketoglutarate.
41
what enzyme is used to get from isocitrate to alpha ketoglutarate + what else does this do
we use isocitrate dehydrogenase to decarboxylate then oxidise isocitrate to form alpha ketoglutarate. which also forms NADH + CO2
42
whats the driving force for the isocitrate to alpha ketoglutarate reaction : decarboxylation and oxidation to form a ketone from the OH ( we remove the CO2 on the 3rd carbon and tuen the OH on the secondd carbon into a ketone)
the CO2 production is the driving froce for the reaction.
43
what is formed from the alpha ketoglutarate
succinyl coenzyme A
44
along with alpha ketoglutarate,, what else do we need to form succinyl coenzyme A.
- alpha keto glutarate - CoA - NAD+ - alpha ketoglutarate dehydrogenase (made up of 3 enzymes - TPP decarboxylation, lipoamideoxidation, transesterification with acetyl coenzymeA) forms Succinyl CoA. + CO2 + NADH