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BMSC 200 > Chapter 5 > Flashcards

Chapter 5 Flashcards

1
Q

For myoglobin and hemoglobin, which ones the storage of oxygen and which ones the delivery?

A 
Hemoglobin= delivery
Myoglobin= storage
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2
Q

What is a protein ligand?

What is oxygen a ligand for?

A

The molecule which is reversible bound by the protein
Can be any kind of molecule
In enzymes the ligand is called the substrate

Oxygen is a ligand for myoglobin and hemoglobin

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3
Q

Where does a ligand bond on a protein?

A

The binding site

This is complimentary in size and shape to the ligand

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4
Q

What other ligand does hemoglobin have besides oxygen?

A

2,3 bisphosphoglycerate

2,3 BPG

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5
Q

What effects of an induced fit of a ligand to a protein cause?

A

Can change the properties of the protein and therefore a new function
Change in structure->change in function

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6
Q

What is myoglobin?

A 
Monomeric protein that facilitates oxygen storage in peripheral tissue
Binary event
Can take oxygen from hemoglobin
Has high affinity for oxygen 
Example of tertiary structure
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7
Q

What is hemoglobin?

A

Tetrametric protein found in erythrocytes that transports oxygen from lungs to the periphery
4 subunits that oxygen can bind to (subunits structurally similar to myoglobin)
Example of quaternary structure

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8
Q

What limits the size of organisms?

A

The amount of available (or usable) oxygen
Insects grown in the presence of elevated oxygen often achieve greater sizes

BUT as you get bigger, it’s harder to maintain oxygen transport system

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9
Q

What are heme oxygen-binding groups?

A

A protoporphyrin ring system bound to a single (Fe2+) iron atom
Fe2+ binds oxygen reversible while Fe3+ does not
Provides four coordinating interactions with the iron atom

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10
Q

What proteins use the heme oxygen-binding group?

A

Myoglobin and hemoglobin

Hemoglobin is essentially 4 myoglobin stuck together (essentially)

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11
Q

How many coordinating interactions does Fe2+ seek?

What are they?

A

Seeks 6 coordinating interactions

  • 4 come from interactions with four groups of heme ring
  • 5th comes from imidazole group of proximal histidine
  • 6th is for O2 binding
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12
Q

Why is carbon monoxide dangerous?

A

It has similar molecular structures as oxygen
Competes with oxygen for binding to heme
CO bonds with 200 times greater affinity than O2

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13
Q

What was the first protein structure to be determined through x Ray crystallography?

A

Sperm whale myoglobin was the first since it is a rich source of myoglobin that can hold for long periods of time

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14
Q

What is the structure of myoglobin?

A

A single polypeptide of 153 residues arranges in eight α-helices
And a heme prosthetic group

Picture in lecture 5 just under halfway

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15
Q

What an oxygen-saturation curve?

A

A graph of the decimal percent saturation with oxygen (Y) over the partial pressure of oxygen (pO2) in torr

Look at myoglobin and hemoglobin saturation curves in lecture 5 at halfway point

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16
Q

What is the P50 mark on a oxygen saturation curve?

A

The amount of O2 required to half saturate the protein

P50 of myoglobin is 3 torr

17
Q

What is the equation used to calculate the fraction of myoglobin saturated with oxygen at a given partial pressure of oxygen?

A

θ= [pO2] / ([PO2] + [P50])

Examples on lecture 5 mid way point

18
Q

What does myoglobins high affinity for oxygen mean for its saturation with oxygen everywhere in the body?

A

High affinity for oxygen= nearly completely saturated with oxygen everywhere within the body under normal circumstances

19
Q

What does allosteric mean?

What is an allosteric protein?

A

Greek word for other shape

Allosteric proteins have Active (R state) and inactive (T state) forms that are in rapid equilibrium

20
Q

What are allosteric effectors?

Modulators

A

They bind to allosteric proteins at sites separate from the functional binding site
Can be activators or inhibitors

21
Q

What do allosteric activators do compares to allosteric inhibitors?

A

Activators- stabilize R state

Inhibitors- stabilize T state

22
Q

What is a homotropic interaction compared to a heterotropic?

A

Homotropic- when normal ligand and modulator are the same

Heterotropic- when the modulator is different from the normal ligand

23
Q

What’s the difference in tissue and lung saturation with a protein that binds O2 with high and constant affinity compared to a protein that binds O2 with a lower affinity?
How does hemoglobin fix this?

A

High O2 affinity- saturate effectively with O2 in lungs but not release it to the tissue
Low O2 affinity- would be able to release O2 to the tissues but not have sufficient affinity to saturate the lungs

Hemoglobin fixes by undergoing transition from a low affinity state to a high affinity state

Look at graph just over halfway of lecture 5

24
Q

What is the homotropic allosteric activator of hemoglobin?

How does it work?

A

O2 is

Example:
The four subunits of hemoglobin are in the T state then when one O2 binds to a T is changes it to R state and eventually all four subunits have O2’s on them and are all turned into R state
Diagram on lecture 5 just over half

25
Q

How does the structure of hemoglobin change when O2 binds and changes it to R state?

A

The iron atom moves from just outside the plane of the heme ring to inside the plane of the heme ring

This causes major quaternary structure changes

26
Q

What decreases hemoglobin affinity for oxygen?

Is it an inhibitor or activator?

A

2,3 Biphosphoglycerate
2,3 BPG

It is a heterotropic allosteric inhibitor of hemoglobin

27
Q

How does 2,3 BPG bind to hemoglobin?

A

It has five units of negative charge and binds to the positively charged pocket that is formed at the interface between the subunits of deoxyhemoglobin

28
Q

How does fetal hemoglobin and 2,3 BPG residues compares to adult hemoglobin and 2,3 BPG residues?

A

Fetal- higher oxygen affinity
Has five 2,3 BPG residues
Adult- lower oxygen affinity
Has six 2,3 BPG residues

29
Q

How does your body adapt to high altitude?

A

There is less oxygen so your body produces more BPG, increases BPG decreases Hb’s O2 affinity
You tire more easily since hemoglobin only comes back to lungs with less than 50% oxygen

30
Q

What is the Bohr effect?

A

Describes the pH dependence of hemoglobins affinity of O2

At decreases pH hemoglobin has a lower affinity for O2

31
Q

What are the two primary mechanisms through which active tissues have lower pH than resting tissues?

A
  1. During moderate exercise, increased muscle activity increases the rate of the CO2 production
  2. In extreme exercise, muscle produce lactic acid to further decrease pH
32
Q

What are the two primary challenges to cellular respiration and metabolism?

A
  1. Providing sufficient O2 to the tissues

2. Removing CO2 from the periphery

33
Q

What is the first mechanism of coordination of O2 delivery and CO2 removal?
(Red blood cell + CO2)

A

CO2 is taken up into the red blood cells (where Hb is located) and converted to bicarbonate and a proton
CO2 + H2O -> H + HCO
-CO2 is concerted to a soluble form
-hemoglobins O2 affinity is increased

34
Q

What is the second mechanism of coordination of O2 delivery and CO2 removal?

A

CO2 forms a covalent linkage to the N terminus of each chain of hemoglobin to form carbaminohemoglobin

  • converts CO2 to more soluble
  • promotes O2 release by lowering O2 affinity
  • proton releases contributes to O2 release
35
Q

How does sickle cell start?

A

Results from single amino acid change

Deforms blood cells

36
Q

How does malaria affect us?

A

Infects red blood cells and decreases pH in the cells which causes release of oxygen from Hb

37
Q

What is hemocyanin?

A

Can be used as a replacement for hemoglobin
Used copper instead of iron
Two coppers bind to single oxygen
No heme ring

BMSC 200 (11 decks)

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