Respiratory Pigments Flashcards

1
Q

What are respiratory pigments?

A

Proteins that increase the oxygen carrying capacity of the blood

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2
Q

What type of proteins are respiratory pigments?

A

Metalloproteins

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3
Q

What do respiratory pigments do?

A

They contain metal ions that reversibly binds to oxygen to increase the amount of oxygen able to be transported by the blood

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4
Q

Why do respiratory pigments have colour?

A

The metal ion

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5
Q

How do respiratory pigments increase the blood carrying capacity of oxygen?

A

They take oxygen out of solution and maintain the pressure gradient from the respiratory surface to the blood

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6
Q

What are the 3 types of respiratory pigments found in animals?

A

Hemoglobin, chlorocruorins and hemocyanins

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7
Q

What colour is hemoglobin? What metal ion does it use to bind oxygen?

A

Red, uses iron in a heme group

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8
Q

Is hemoglobin intracellular or extracellular?

A

Can be either

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9
Q

What colour are chlorocruorins? What metal ion does it use to bind oxygen?

A

Green-ish red. They use iron, but not as a heme

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10
Q

What organisms are chlorocruorins found in?

A

A few families of marine worms

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11
Q

Are chlorocruorins intracellular or extracellular?

A

Extracellular

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12
Q

Are chlorocruorins related to hemoglobin?

A

Yes, a subclass of the same family

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13
Q

What colour are hemocyanins? What metal ion does it use to bind oxygen?

A

Blue. They use copper

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14
Q

What colours are hemocyanins when they are deoxygenated vs oxygenated?

A

Colourless when deoxygenated and blue when oxygenated

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15
Q

Are hemocyanins related to hemoglobin?

A

No, they evolved independently

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16
Q

How many oxygen molecules bind per heme?

A

One

17
Q

How many subunits and oxygen binding sites are in hemoglobin?

A

4 subunits: 2 alpha and 2 beta. Each subunit has a heme so 4 oxygen binding sites

18
Q

What type of binding curve is seen for hemoglobin?

A

Sigmoidal

19
Q

Why does hemoglobin have a sigmoidal binding curve?

A

It shows cooperativity

20
Q

What state is hemoglobin in when it is deoxygenated? What bonds are stabilizing this state? How much of an affinity for oxygen does it have?

A

The T state. Stabilized by salt bridges and hydrogen bonds. Low oxygen affinity

21
Q

What state is hemoglobin in when it is oxygenated? What bonds are stabilizing this state? How much of an affinity for oxygen does it have?

A

The R state. Stabilized only by hydrogen bonds. High oxygen affinity

22
Q

Why does oxygen binding cause a conformation change in the hemoglobin subunits?

A

It weakens the salt bridges

23
Q

What determines the percentage of hemoglobin saturation?

A

Partial pressure of oxygen

24
Q

What is the oxygen partial pressure in the alveoli, cells, and blood?

A

High pressure in the alveoli, low in the cells and blood

25
Q

What is the carbon dioxide partial pressure in the alveoli, cells, and blood?

A

Low pressure in the alveoli and blood, high in the cells

26
Q

What is pulmonary circulation?

A

Circulation between the heart and lungs

27
Q

What is systemic circulation?

A

Circulation between the heart and the rest of the body

28
Q

How much of the total oxygen in the blood is carried by hemoglobin (%)?

A

98.5%

29
Q

What is the maximum oxygen saturation in the pulmonary and systematic capillaries? Why are they different?

A

Pulmonary: 97%
Systematic: 75%
Pulmonary circuit has more hemoglobin in it

30
Q

What defines the affinity of hemoglobin to oxygen?

A

The P50: the oxygen pressure when hemoglobin is 50% saturated. = Km

31
Q

What is the oxygen affinity of hemoglobin when P50 is low?

A

High affinity

32
Q

What is the oxygen affinity of hemoglobin when P50 is high?

A

Low affinity

33
Q

Is P50 constant?

A

No, changes depends on what is happening in the body

34
Q

What is the P50 of myoglobin? Why is this an adaptation?

A

Very low, so it has high affinity to oxygen. It allows myoglobin to pull oxygen off of hemoglobin and into the cells