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Chemistry Fall 24' > Final Review Cards/Questions > Flashcards

Final Review Cards/Questions Flashcards

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1
Q

What is the primary function of myoglobin (Mb)?

A

Stores and transports oxygen in muscles

Myoglobin provides oxygen for metabolic processes to convert/produce energy.

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2
Q

How does myoglobin respond to muscle activation?

A

Desaturates upon muscle activation

This process increases diffusion from capillaries to the cytoplasm.

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3
Q

What is the role of hemoglobin (Hb)?

A

Transports oxygen from the lungs to tissue

Hemoglobin also transports carbon dioxide from tissue to lungs.

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4
Q

What is the affinity of hemoglobin for oxygen and carbon dioxide?

A

High affinity for oxygen; low affinity for carbon dioxide

In venous circulation, hemoglobin has a high affinity for carbon dioxide.

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5
Q

What type of bonds are primarily found in single bonds?

A

Sigma bonds

Sigma bonds are formed by the head-on overlap of atomic orbitals.

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6
Q

What is the oxidation state of iron in heme?

A

Either Fe2+ or Fe3+

Iron’s oxidation state is crucial for its function in binding oxygen.

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7
Q

What are ligands?

A

Electron-rich species that coordinate to metal ions

Ligands help stabilize charge and solubilize metal ions.

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8
Q

What structure do iron complexes typically form?

A

Stable octahedral complexes

This is based on the hybridization of the metal center.

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9
Q

What are porphyrins?

A

Heterocyclic macrocycles composed of four modified pyrrole subunits

Porphyrins are highly conjugated aromatic compounds found in mammals, plants, and bacteria.

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10
Q

What is the structure of protoporphyrin IX?

A

Contains heme

Protoporphyrin IX is crucial for the function of hemoproteins.

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11
Q

What is an apoprotein?

A

Unbound protein that is inactive

Apoproteins are necessary for heme to become water soluble.

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12
Q

What is the quaternary structure of hemoglobin?

A

Tetrameric structure

Fetal hemoglobin has a different structure with higher affinity than adult hemoglobin.

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13
Q

True or False: Carbon monoxide (CO) binds better than oxygen (O2) to heme.

A

True

CO binds to the same site as O2 but with a much higher affinity.

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14
Q

Fill in the blank: Myoglobin is a _______ heme protein.

A

monomeric

This indicates that myoglobin consists of a single polypeptide chain.

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15
Q

What is the significance of the coordination sites in iron?

A

Contains six coordination sites

These sites are based on the hybridization of the metal center and are important for binding ligands.

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16
Q

What is the main role of heme complexes?

A

Enhance water solubility of heme

Heme complexes are fairly insoluble on their own.

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17
Q

What is the term for the protein that carries oxygen in the blood?

A

hemoglobin

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18
Q

What type of curve does hemoglobin exhibit in its oxygen binding?

A

Sigmoidal curve

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19
Q

True or False: Hemoglobin has a higher affinity for O2 when it is in a relaxed state.

A

t

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20
Q

Fill in the blank: Hemoglobin exhibits _______ cooperation in oxygen binding.

A

cooperative

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21
Q

What effect does 2,3-Bisphosphoglycerate (BPG) have on hemoglobin’s affinity for oxygen?

A

It decreases affinity

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22
Q

What is meant by a leftward shift in the oxygen dissociation curve?

A

Increased affinity for the ligand

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23
Q

What state of hemoglobin is associated with higher oxygen binding?

A

Relaxed state

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24
Q

What is the role of competitive inhibitors in relation to hemoglobin and oxygen?

A

Compete with O2 but help maintain hemoglobin’s structure

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25
Q

True or False: Increasing O2 pressure will decrease the binding of CO to hemoglobin.

A

t

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26
Q

What is the impact of CO2 on hemoglobin’s oxygen binding?

A

It can promote the release of O2

27
Q

Fill in the blank: Hemoglobin has _______ affinity for unbound heme.

A

increased

28
Q

What happens to hemoglobin’s oxygen affinity when it is in a bound state?

A

It has a lower affinity for O2

29
Q

What is the term for the protein that carries oxygen in the blood?

A

hemoglobin

30
Q

What type of curve does hemoglobin exhibit in its oxygen binding?

A

Sigmoidal curve

31
Q

True or False: Hemoglobin has a higher affinity for O2 when it is in a relaxed state.

A

t

32
Q

Fill in the blank: Hemoglobin exhibits _______ cooperation in oxygen binding.

A

cooperative

33
Q

What effect does 2,3-Bisphosphoglycerate (BPG) have on hemoglobin’s affinity for oxygen?

A

It decreases affinity

34
Q

What is meant by a leftward shift in the oxygen dissociation curve?

A

Increased affinity for the ligand

35
Q

What state of hemoglobin is associated with higher oxygen binding?

A

Relaxed state

36
Q

What is the role of competitive inhibitors in relation to hemoglobin and oxygen?

A

Compete with O2 but help maintain hemoglobin’s structure

37
Q

True or False: Increasing O2 pressure will decrease the binding of CO to hemoglobin.

A

t

38
Q

What is the impact of CO2 on hemoglobin’s oxygen binding?

A

It can promote the release of O2

39
Q

Fill in the blank: Hemoglobin has _______ affinity for unbound heme.

A

increased

40
Q

What happens to hemoglobin’s oxygen affinity when it is in a bound state?

A

It has a lower affinity for O2

41
Q

Primary function of myoglobin?

A

Store and transport oxygen into muscles

42
Q

What oxidation states can iron exist in heme proteins?

A

Fe2+(ferrous) and Fe3+(ferric)

43
Q

Hybridization of iron in heme proteins?

A

sp3d2

44
Q

How nmany coordination sites does iron have in heme proteins?

A

6

45
Q

What type of structure is formed when all ligands are bound to iron in heme proteins?

A

Octahedral

46
Q

Term for an unbound protein that is inactive?

A

apoprotein

47
Q

Amino acid residue that binds to the fifth coordination site of iron in heme proteins?

A

Histidine

48
Q

Structural difference between hemoglobin and myoglobin?

A

Myoglobin is monomeric and hemoglobin is a tetrameric

49
Q

What level of protein structure is represented by a single myoglobin unit?

A

Tertiary

50
Q

What level of protein structure is represented by hemoglobin?

A

Quaternary

51
Q

What is the hill coefficient for hemoglobin?

A

2.7

52
Q

Which state of hemoglobin is known as the tense state?

A

T State

53
Q

What is the main difference between fetal and adult hemoglobin?

A

fetal hemoglobin has gamma subunits instead of beta. (Both have Alpha)

54
Q

Why does fetal hemoglobin have a higher affinity for oxygen compared to adult hemoglobin?

A

Because it has more alpha subunits

55
Q

What percentage of CO2 is transported as dissolved gas in blood plasma?

A

0.1

56
Q

What is the effect of increasing temp on oxygen binding to hemoglobin?

A

Increases oxygen dissociation

57
Q

What is formed when CO2 binds to the N-terminal group of hemoglobin?

A

Carbamate

58
Q

How many times more strongly does carbon monoxide bind to hemoglobin compared to oxygen?

A

200-300 times

59
Q

What happens to oxygen affinity when blood pH decreases?

A

Decreases

60
Q

What is the main reason hydroxide cannot deprotonate water?

A

Water is the conjugate acid of hydroxide

61
Q

What must be true for hydroxide to deprotonate a compound?

A

The pKa must be below 16

62
Q

What determines if a compound is an aniline?

A

The NH2 group MUST be attached to a BENZENE ring

63
Q

To be an H-Bond acceptor, N or O must have what?

A

A lone pair of electrons

Chemistry Fall 24' (8 decks)

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