Bios 3200 Exam 2

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Last updated 1:09 AM on 9/24/26
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50 Terms

1
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where is the majority (~80%) of ATP produced?

mitochondria

2
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what are the two membranes of the mitochondria?

inner and outer membranes

3
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what are the two spaces of the mitochondria?

matrix and intermembrane space

4
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the inner membrane of the mitochondria has a __________ _________ system to make H+ gradient

electron transport

5
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the inner membrane is full of ______, but it is not _____

proteins, rigid

6
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the mitochondria is flexible, and it is continuously _________, _____________, and __________

moving, dividing, fusing

7
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why are cristae formed?

inner membrane of mitochondria needs a large surface area

8
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what does the mitochondrial matrix contain enzymes for?

citric acid cycle

9
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what does the mitochondrial outer membrane contain?

porin - free pass for small molecules (<1000 daltons)

10
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where does glycolysis occur?

cytosol

11
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in glycolysis, what are the net products for 1 molecule of glucose?

2 pyruvate, 2 ATP, 2 NADH

12
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what forms acetyl-CoA?

when the acetyl group of pyruvate is transferred to CoA (coenzyme A)

13
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the citric acid cycle oxidizes all carbon to _____

CO2

14
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what are the products made after glycolysis/citric acid cycle per 1 pyruvate?

4 NADH, 1 FADH2, 1 GTP (= 1 ATP), 3 CO2

15
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where does the citric acid cycle occur?

mitochondrial matrix

16
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NAD

nicotinamide adenine dinucleotide

17
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NAD+

oxidized form, nicotinamide ring has 1 H and positive charge on nitrogen

18
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NADH

reduced form (high energy state), nicotinamide ring has 2 H and no charge on nitrogen

19
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what is redox potential?

how energetically favorable it is to reduce (give electron to) other chemicals; strength as an electron donor

20
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what is the mechanism/order of operations for the electron transport chain (complexes I-IV)?

  1. electron pairs from NADH are received at complex I and are then transferred to ubiquinone (Co-Q)

  2. electron pairs from FADH2 are received at complex II and are then transferred to Co-Q

  3. Co-Q carriers the electrons to complex III, which then transfers the electrons to cytochrome C

  4. cytochrome C carries the electron pairs to complex IV where they reduce O2 and produce H2O


21
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which complexes are H+ pumped out of into the intermembrane space?

complexes I, III, IV

22
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how many H+ does complex I pump out?

4

23
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how many H+ does complex III pump out?

4

24
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how many H+ does complex IV pump out?

4

25
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what are the 2 electron carriers in the ETC?

ubiquinone (Co-Q) and cytochrome C

26
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ubiquinone (Co-Q)

permanently embedded in inner membrane; can receive two electrons with two protons

27
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what does the reduced form of ubiquinone look like?

has 2 OH groups opposite of each other (high energy)

28
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what does the oxidized form of ubiquinone look like?

has 2 double bonded O opposite of each other (low energy)

29
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what is the chemiosmatic theory?

free energy is created by H+ electrochemical gradient

energy can be used for ATP generation

not metabolic ATP synthesis; closed membrane is essential for the reaction, pH change affects ATP synthesis by isolated mitochondria

30
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what are the other 2 names for F1F0 ATPase?

ATP synthase, complex V

31
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what does ATP synthase do? (basic)

convert electrochemical gradient of H+ into ATP; final step of ATP synthesis

32
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what are the two main parts of ATP synthase?

F1 and F0

33
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what is F0?

transmembrane H+ carrier

34
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what is the structure of F0?

12 c-subunits, form c-ring

1 a-subunit

2 b-subunits

35
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what is F1?

catalytic component of ATP synthase

36
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what is the structure of F1?

(αβ)3 and γ stalk

37
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(αβ)3 structure and function?

spherical structure; has ATPase activity

38
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γ stalk

rotor stalk; connects c-ring (tightly associated) to (αβ)3 (loosely associated, sits deep in)

39
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what is the F1F0 ATPase basic mechanism? (2 steps)

  1. while H+ passes through F0, the rotor rotates relative to the stator; H+ gradient → rotation

  2. while rotor rotates, F1 synthesizes ATP from ADP and phosphate; rotation → ATP synthesis


40
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explain the mechanism of F0 rotation (4 steps)

  1. a-subunit has two half-channels for H+; H+ enters in first channel from intermembrane space/outside the mitochondria

  2. each c-subunit has a proton-acceptor, which receives proton from a half-channel

  3. after accepting proton, c-ring slides by one subunit, then next H+ comes through the half-channel and binds next c-subunit, then c-ring rotates by one subunit….

  4. after one round of rotation (12 H+), H+ is transferred from c-subunit to another half-channel that is open to the opposite side


41
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how does rotation of the γ stalk make ATP in F1?

as γ stalk rotates in F1 ATPase, three αβ subunits change conformation

42
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what are the 3 conformations that the γ stalk can change the αβ subunits to?

open, tight, low-affinity conformations

43
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O (open) conformation

has low affinity to ATP and can exchange ATP/ADP; will release ATP and then bind ADP + Pi

44
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T (tight) conformation

can only bind ATP, never release it; converts ADP + Pi to ATP

45
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L (low-affinity) conformation

binds ADP and Pi, but they can’t escape form the protein

46
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how many ATP are produced per one complete turn of the γ stalk in F1 ATPase?

3

47
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___ H+ can produce ___ ATP

4, 1

48
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how many H+ and ATP can one matrix NADH produce?

12 H+ and 3 ATP

49
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how many H+ and ATP can one FADH2 produce?

8 H+ and 2 ATP

50
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how many H+ and ATP can one cytosolic NADH produce? (60% efficient)

7.2 H+ and 1.8 ATP