Brainscape's Knowledge GenomeTM

Browse over 1 million classes created by top students, professors, publishers, and experts.


See full index

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Oxygen is the final electron acceptor in ?

A

ETC

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

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

A

lower

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

energy released by electrons generates?

A

electrochemical gradient (H+ gradient)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Oxidized

A

loss electron

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

Reduced

A

gain electron

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Reduction potential

A

affinity for electrons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Low reduction potential means

A

low affinity for electrons

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Electrons are being transferred from molecules of ______ potential to _____

A

low to high

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

T/F: electrons acceptors are more negative

A

false; acceptors are more positive

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Chemiosmotic Coupling

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Electrochemical gradient provides energy for?

A

ATP Synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

ETC is made up of ____ complexes and _____ proton pumps

A

4;3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What are the two mobile electrons carriers in the ETC?

A

Q and Cytochrome C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Complex 1 allows _____ to enter

A

NADH

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

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

A

3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

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

A

complex 2; 6

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

How many ATP are produced per FADH2?

A

2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

List the electron carriers that move electrons between complexes

A

Ubiquinone, Cytochromes, Iron-Sulfur Centers

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
23
Q

Ubiquinone

A

carriers two electrons at a time; small and hydrophobic

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
24
Q

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

A

ubiquinone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
25
Q

Cytochromes contain what group?

A

Contains heme group (porphyrin ring with Fe bound)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
26
Q

How many electrons do cytochromes carry at a time?

A

1

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
27
Q

Iron-Sulfur centers

A

1 electron center

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
28
Q

Cytochrome C transports electrons from complex ___ to ____

A

3 to 4

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
29
Q

Complex 1 AKA

A

NADH dehydrogenase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
30
Q

Complex 1

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
31
Q

Complex 2 AKA

A

Succinate Dehydrogenase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
32
Q

Complex 2

A

FADH2 oxidized to FADno proton pumpingDonor: FADH2Acceptor: Ubiquinone

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
33
Q

Complex 3 AKA

A

Cytochrome b-c1 complex

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
34
Q

Complex 3

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
35
Q

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

A

2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
36
Q

Complex 4 AKA

A

Cytochrome oxidase

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
37
Q

Complex 4

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
38
Q

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

A

True

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
39
Q

For 1 NADH we get ___ ATP

A

3

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
40
Q

For 1 FADH2 we get ___ ATP

A

2

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
41
Q

ATP Synthase has ___ parts

A

Two; F1 & FO

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
42
Q

F0 in ATP Synthase

A

in the membrane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
43
Q

F1 in ATP Synthase

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
44
Q

F1 Complex

A

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

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
45
Q

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

A

beta

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
46
Q

Where does reactions occur?

A

beta subunit

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
47
Q

What drives ATP Synthesis?

A

rotational catalysis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
48
Q

What are the three subunits?

A

empty–ready to accept ADP (phosphate)ADPATP

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
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?

53
Q

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

54
Q

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

55
Q

Excess sugar is stored as

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)?

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

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?

73
Q

Amino group

74
Q

Carboxyl Group

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?

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

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

88
Q

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

89
Q

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

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 _______

94
Q

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

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?

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?

115
Q

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

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?

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)

Brainscape helps you reach your goals faster, through stronger study habits.
© 2025 Bold Learning Solutions. Terms and Conditions