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Biochemistry > ETC, ATP Synthesis, & Amino Acid Structure > Flashcards

ETC, ATP Synthesis, & Amino Acid Structure Flashcards

1
Q

Where is the electron transport chain located?

A

inner mitochondrial membrane

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2
Q

What does the ETC do?

A

uses electrons from NADH and FADH2 produced by glycolysis, pyruvate dehydrogenase, and citric acid cycle for the production of ATP and then it regenerates FAD and NAD+ under aerobic conditions

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3
Q

Oxygen is the final electron acceptor in ?

A

ETC

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4
Q

Which each transfer of electrons, they get transfered to a ______ energy state

A

lower

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5
Q

energy released by electrons generates?

A

electrochemical gradient (H+ gradient)

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6
Q

Oxidized

A

loss electron

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7
Q

Reduced

A

gain electron

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8
Q

Reduction potential

A

affinity for electrons

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9
Q

Low reduction potential means

A

low affinity for electrons

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10
Q

Electrons are being transferred from molecules of ______ potential to _____

A

low to high

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11
Q

T/F: electrons acceptors are more negative

A

false; acceptors are more positive

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12
Q

Chemiosmotic Coupling

A

coupling between membrane transport and chemical bond formation (Mitochondrial matrix to intermembrane space)

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13
Q

Give an example of chemiosmotic coupling involving the ETC and ATP Synthase

A

Electron transport drives pump that pumps protons across membrane, proton gradient is then harnessed by ATP Synthase to make ATP

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14
Q

Electrochemical gradient provides energy for?

A

ATP Synthesis

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15
Q

ETC is made up of ____ complexes and _____ proton pumps

A

4;3

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16
Q

What are the two mobile electrons carriers in the ETC?

A

Q and Cytochrome C

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17
Q

Complex 1 allows _____ to enter

A

NADH

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18
Q

If it starts with NADH what complexes will it move through and how many protons will move to the intermembrane space?

A

1, 3, & 4; 10 protons

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19
Q

How many ATP are produced per NADH that enters the ETC?

A

3

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20
Q

Where does FADH2 enter? and pumps how many protons across the membrane?

A

complex 2; 6

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21
Q

How many ATP are produced per FADH2?

A

2

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22
Q

List the electron carriers that move electrons between complexes

A

Ubiquinone, Cytochromes, Iron-Sulfur Centers

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23
Q

Ubiquinone

A

carriers two electrons at a time; small and hydrophobic

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24
Q

Carriers electrons from complex 1 to complex 3 and complex 2 to complex 3

A

ubiquinone

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25
Q

Cytochromes contain what group?

A

Contains heme group (porphyrin ring with Fe bound)

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26
Q

How many electrons do cytochromes carry at a time?

A

1

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27
Q

Iron-Sulfur centers

A

1 electron center

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28
Q

Cytochrome C transports electrons from complex ___ to ____

A

3 to 4

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29
Q

Complex 1 AKA

A

NADH dehydrogenase

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30
Q

Complex 1

A

Donor: NADH Acceptor: Ubiquinone4 Protons pumped into intermembrane space per electron pair

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31
Q

Complex 2 AKA

A

Succinate Dehydrogenase

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32
Q

Complex 2

A

FADH2 oxidized to FADno proton pumpingDonor: FADH2Acceptor: Ubiquinone

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33
Q

Complex 3 AKA

A

Cytochrome b-c1 complex

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34
Q

Complex 3

A

pumps 4H+ across membrane acceptor: cytochrome CDonor: ubiquinone Electrons are passed from QH2 to cyctochrome C1 via electron

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35
Q

For every pair of electrons that come from ubiquinone we end up having ____ cytochrome C

A

2

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36
Q

Complex 4 AKA

A

Cytochrome oxidase

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37
Q

Complex 4

A

final redox reaction in ETCacceptor: oxygen output: 2 H20cytochrome C1 brings electrons in one at a time

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38
Q

T/F: Pumping of protons is endergonic and the discharge of the gradient is exergonic

A

True

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39
Q

For 1 NADH we get ___ ATP

A

3

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40
Q

For 1 FADH2 we get ___ ATP

A

2

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41
Q

ATP Synthase has ___ parts

A

Two; F1 & FO

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42
Q

F0 in ATP Synthase

A

in the membrane

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43
Q

F1 in ATP Synthase

A

peripheral membrane protein, plugs FO so proton gradient can form (really occurs)

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44
Q

F1 Complex

A

Alternating alpha and beta subunits. Gamma subunit is the central section

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45
Q

Each ___ subunit has a different conformation and a different ability to bind ADP/ATP

A

beta

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46
Q

Where does reactions occur?

A

beta subunit

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47
Q

What drives ATP Synthesis?

A

rotational catalysis

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48
Q

What are the three subunits?

A

empty–ready to accept ADP (phosphate)ADPATP

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49
Q

Gamma subunits rotate in which direction as protons are pumped across

A

counter clockwise

50
Q

Contransport of what is required for ATP Synthesis?

A

H+ and phosphate

51
Q

What drives the exchange of ADP for ATP due to an electrochemical gradient?

A

voltage difference

52
Q

The net yield from glucose is?

A

36 ATP

53
Q

NADH from glycolysis results in a lower/higher ATP yield than other NADH

A

lower

54
Q

If complex 2 is not functioning, how much less ATP would be produced per glucose?

A

4 fewer

55
Q

Excess sugar is stored as

A

glycogen

56
Q

Storage of glycogen is primarily in the:

A

liver and muscle

57
Q

Where does the breakdown of fatty acids occur?

A

Mitochondria

58
Q

Each round of fatty-acid oxidation cycle releases:

A

1 acetyl-CoA1 NADH1 FADH2

59
Q

How many ATP would be produced as a result of one cycle of fatty acid oxidation (not taking into account of the citric acid cycle)?

A

5

60
Q

Where is Acetyl-CoA derived from?

A

breakdown of carbohydrates and fats feeds into the citric acid cycle

61
Q

Glycolysis and Cancer

A

Glycolysis goes faster than normal because there is a limited O2 supplythe cells take up more glucose than normal cells due to more transporterscompounds that inhibit steps of glycolysis are often used in treatment

62
Q

Glycolysis and Type 1 Diabetes

A

too few beta cells in the pancreas cause low insulin levels, leading to insufficient uptake of glucose by cells. can lead to lowered blood pH due to products of fatty acid oxidation

63
Q

lowered blood pH

A

Ketoacidosis

64
Q

Glycolysis and Type 2 Diabetes

A

development of insulin resistance- more insulin is required to achieve the same effects

65
Q

When are ketone bodies produced?

A

prolonged fast or starvation (glucose is unavailable, glycogen deplettion, and gluconegenesis occurs)

66
Q

Gluconeogenesis

A

glucose synthesis, uses acetoacetate to try to make glucose.

67
Q

Ketone bodies function as

A

acids, which makes blood more acidic

68
Q

When we dont have glucose for a long period of time… our bodies try to make

A

glucose

69
Q

What are the levels of protein structure?

A

Primary, Secondary, Teritary, Quaternary

70
Q

Primary structure is

A

the sequence of amino acids

71
Q

Amino acids have its central carbon bonded to what and how

A

covalently bonded to 4 groups

72
Q

how many different amino acids are there?

A

20

73
Q

Amino group

A

H2N

74
Q

Carboxyl Group

A

COOH

75
Q

Amino Acid structure rubric

A

H2N–CHR–COOH

76
Q

What are the four families of amino acids?

A

Basic Positive, Acidic Negative, Uncharged Polar and Nonpolar

77
Q

How are amino acids linked to eachother?

A

via condensation reactions that result in the formation of peptide bonds

78
Q

Are peptide bonds planar?

A

Yes

79
Q

T/F: Peptide bonds have a partial double bond character, allowing rotation.

A

False. The partial double bond character prevents rotation.

80
Q

conformation:

A

shape of a folded protein

81
Q

proteins try to fold in a way that minimizes/maximizes free energy

A

minimizes

82
Q

What type of bonds give proteins its shape?

A

noncovalent

83
Q

Why are nonpolar (hydrophobic) R groups forced together?

A

to minimize interference with H-bonding between water molecules

84
Q

Cellular Respiration: List 3 stage

A
  1. Generation of Acetyl-CoA2. Citric Acid Cycle3. ETC
85
Q

secondary structure:

A

stretches of a protein that forms alpha helices and beta sheets

86
Q

alpha helix

A

polypetitide chain twists to form a cylindersecondary structure

87
Q

alpha helices occur ____amino acids/turn

A

3.6

88
Q

amino groups forms a H-bond with the carboxyl group at the _____ position

A

n+4

89
Q

each strand of a beta sheet has a pleat ever ____ amino acids

A

2

90
Q

What are the two subtypes of beta sheets?

A

Antiparallel & parallel

91
Q

tertiary structure

A

3D arrangement of secondary elements connected by loops

92
Q

what stablizes tertiary structure?

A

noncovalent interactions and disulfide bonds

93
Q

Amino Acid Location: Nonpolar tends to be _______

A

interior

94
Q

Amino Acid Location: Polar charged tend to be on the ______

A

surface

95
Q

Amino Acid Location: Polar uncharged tend to be ______

A

found on the interior and on the surface

96
Q

What are the two classes of tertiary structure?

A

Fibrous and Globular

97
Q

Fibrous Proteins

A

polypeptide chains composed primarly of one type of secondary structure

98
Q

Fibrous Proteins provide

A

strength and stability

99
Q

T/F: Fibrous proteins are not insoluble in water due to the large number of hydrophobic amino acids

A

False. They are insoluble.

100
Q

Examples of Fibrous Proteins

A

Keratin, Fibroin & Collagen

101
Q

Globular Proteins

A

Polypeptide folds into a compact shape with an irregular surface (Mix of secondary structural elements)

102
Q

Are globular proteins water soluble?

A

Yes.

103
Q

What are Globular proteins made up of?

A

Motifs and Domain

104
Q

Motif

A

pattern or arrangment of secondary structure that has been seen multiple times

105
Q

Domain

A

a strech of amino acids that are capable of folding independently of the rest of the polypeptide into a compact and stable structure

106
Q

What is an example of Globular Protein?

A

Src (enzyme with three domains)

107
Q

Protein Folding Chaperones

A

molecular chaperones bind partially folded polypeptides to help them fold, they minimize energy used for the folding process and prevent inappropiate association of unfolded proteins

108
Q

Two types of Chaperones

A

Hsp70 & Hsp60

109
Q

Hsp70

A

smaller, fold as translated, protein still attached to ribosome, energy needed

110
Q

Hsp60

A

larger, occurs after translation, released from ribosome

111
Q

Disulfide Bonds

A

covalent bonds that crosslink parts of a chain or two different chains via adjacent cysteine side chains

112
Q

What do disulfide bonds stabilize?

A

tertiary and quarternary protein structure

113
Q

Protein Disulfide Isomerase (PDI)

A

binds to unfolded/incorrectly folded proteins to allow new bonds to be formed until the correct bonds are formed

114
Q

Give an example of a protein that needs to be cleaved to be functional?

A

Insulin

115
Q

What type of protein is more likely to function as an enzyme?

A

Globular

116
Q

Quarternary Structure

A

protein composed of multiple polypeptides, subunits can be identical or different

117
Q

What is quarternary structure stabilized by?

A

noncovalent interactions and disulfide bonds

118
Q

can subunits of quarternary structure be differeent?

A

Yes

119
Q

Alzheimers Disease results in part to

A

problems in protein folding

120
Q

if a misfolded protein is present, it causes the normally folded protein to misfold leading to

A

disease (the brain develops holes)

Biochemistry (7 decks)

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