Class 6: Oxidative phosphorylation Flashcards

1
Q

what is the major source of one-carbon groups in the human

A

serine

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2
Q

what is a process for the synthesis of ATP and the ,for source of ATP in aerobic organisms

A

oxidative phosphorylation

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3
Q

source of ATP

A

high-energy electrons from NADH or FADH2 (from TCA cycle)

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4
Q

path of OXPHOS

A

accomplished through a number of electron-transfer reactions, which take place in a set of membrane proteins known as the electron transport chain in the mitochondria

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5
Q

results of OXPHOS

A

reduction of oxygen and the generation of a proton gradient (also called proton motive force), which is used to power the synthesis of ATP

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6
Q

location of OXPHOS

A

mitochondria

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7
Q

outer membrane of mitchondria

A

-permeable to most small ions and moleculesbc of Porin(allows passive diffusion

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8
Q

inner membrane of mitochondria

A
  • folded into ridges called cristae
  • impermeable to most molecule
  • the site of electron transport and ATP synthesis
  • FA transport
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9
Q

Intermembrane space of mitochondria

A
  • nucleotide kinase
  • proton gradient
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10
Q

martix of mitochondria

A

the citric acid cycle and and fatty acid oxidation occur in the matrix
- could write more

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11
Q

what takes place in the four large protein complexes embedded in the inner mitochondrial membrane

A

the oxidation-reduction reactions that allow the flow of electrons from NADH and FADH2 to oxygen. Also called the respiratory chain resulting in the reduction of oxygen and the generation of the proton gradient

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12
Q

the electron carriers in the protein complexes include?

A

1) flavin mononucleotide (FMN)
2) iron associated with sulfur in proteins (iron-sulfur proteins),
3) a mobile electron carrier called coenzyme Q (Q).
4) iron incorporated into hemes that are embedded in cytochromes, mobile electron carrier proteins.

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13
Q

ubiquinone

A

oxidized coenzyme in carrier 3

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14
Q

ubiquinol

A

reduced coenzyme in carrier 3

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15
Q

study slide 13-16

A

mmm

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16
Q

Reactive Oxygen Species (ROS)

A

1) Electrons leak at Complex I and III from semiquinone radical

2) Partial reduction of O2 generates highly reactive oxygen derivatives, called reactive oxygen species (ROS).

3) ROS include superoxide ion (O2-), peroxide ion (O22-), and hydroxyl radical (OH).

4) 2%-4% of oxygen molecules consumed by mitochondria are converted into superoxide ions.

17
Q

ros and human disease slide 20

A

jjjj

18
Q

what enzymes protect against ROS damage

A

1) superoxide dismutase
2) Catalase
3) GSH peroxidase

19
Q

ROS

A

superoxide ion, peroxide ion, and hydroxyl radical

20
Q

Other defenses against ROS

A

vitamin E
vitamin C
vitamin A
exercise
-could write descriptions

21
Q

what is the proton motive force

A

The proton gradient generated by the oxidation of NADH and FADH2 is called the proton-motive force, which powers the synthesis of ATP.

22
Q

chemiosmosis hypothesis

A

electron transport and ATP synthesis are coupled by a proton gradient across the inner mitochondrial membrane.

23
Q

electrochemical gradient (proton gradient)

A

drives the formation of proton - motive force : a chemical gradient and a charge gradient.

24
Q

proton motive force formula

A

(Delat p) = chemical gradients + charge gradient

25
Q

F0 component of ATP synthase

A

The F0 component (hydrophobic) is embedded in the inner mitochondrial membrane and contains the proton channel

26
Q

F1 component of ATP synthase

A

The F1 component contains the catalytic activity and protrudes into the mitochondrial matrix.

27
Q

4 steps of proton flow around the c ring powering ATP synthesis

A

1) Subunit a, which abuts the c ring, has two channels that reach halfway into the a subunit. One half channel opens to the intermembrane space and the other to the matrix.
2) Protons enter the half channel facing the proton-rich intermembrane space, bind to an glutamate residue on one of the subunits of the c ring, and then leave the c subunit once they rotate around to face the matrix half channel.
3) The force of the proton gradient powers rotation of the c ring.
4) The rotation of the c ring powers the movement of the γ subunit, which in turn alters the conformation of the β subunits.

28
Q

ability of ASP and GLU side chains to accept protons can be important in ?

A

enzyme catalyst

29
Q

The three catalytic B subunits of the F1 component can exist in what 3 conformations

A

O (open) form: release
L (loose) form: trap
T (tight) formL synthesis

30
Q

how many protons must flow through the matrix for each molecule of ATP to be formed

A

3
- flow though each proton drives 1200degree rotation of B subunit

31
Q

the complete oxidation of glucose yields about how many molecules of ATP

A

30
-glycolysis: 2 ATP
-TCA cycle: 2 ATP
-OXPHOS: ~26

32
Q

the glycerol 3-phosphate shuttle

A

NADH –> FADH2
-in muscle, electrons from cytoplasmic NADH can enter the electron transport chain by using this shuttle
-after the electrons are transferred from NADH to FADH2 they’re subsequently to Q to form QH2

33
Q

the malate-aspartate shuttle

A

NADH –> NADH
-In heart and liver, electrons from cytoplasmic NADH are used to generate mitochondrial NADH in malate-aspartate shuttle.

The malate-aspartate shuttle consists of two membrane transporters and four enzymes.

34
Q

go over slides 34- end

A

k