Haemoglobin Flashcards

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1
Q

What type of protein is haemoglobin

A

Globular

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2
Q

Why is it good that red blood cells do not contain a nucleus

A

Provides more space inside the cell for haemoglobin so that they can transport as much O2 as possible

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3
Q

What structure does haemoglobin have

A

Quaternary made up of 4 polypeptide chains

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4
Q

Describe the globin proteins in a haemoglobin

A

Four globin subunits are held together by disulphide bonds
Arranges so their hyrophobic R groups are facing inwards helping to preserve the three dimensional spheric shape
The hydrophilic R groups face outwards to maintain solubility

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5
Q

What does the haem group contain

A

Fe2+ which is able to reversibly combine with an oxygen molecules to form oxyhaemoglobin

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6
Q

How many oxygen molecules can be carried in a haemoglobin

A

Because of their four haem mgroups they can carry four oxygen molecules or 8 oxygen atoms

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7
Q

What is haemoglobins function

A

Binding oxygen in lungs and transporting the oxygen to the tissue to be used in aerobic metabolic pathways

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8
Q

Why can oxygen be carried efficiently

A

Oxygen isn’t very soluble in water and haemoglobin is

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9
Q

What does the Fe2+ allow when transporting haemoglobin

A

Allows O2 to be reversibly bind
No amino acids that make up the polypeptide chains in haemoglobin are well suited to binding with oxygen

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10
Q

What does the oxygen bind to

A

The haem groups

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11
Q

Whats another word for red blood cells

A

Erythrocytes

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12
Q

Equation for haemoglobins binding to oxygen

A

Oxygen + Haemoglobin <-> Oxyhaemoglobin

4O2 + Hb <-> Hb4O2

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13
Q

Process name of O2 binding

A

Cooperative bindig

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14
Q

Describe cooperative binding

A

Binding of first O2 molecule results in conformational change in the structure of the haemoglobin molecule
so its easier for each successive O2 to bind

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15
Q

How are red blood cells adapted for O2 transport

A

Red blood cells lack nuclei = more space for haemoglobin
Biconcave shape = high SA:V, so there is a short diffusion distance for O2

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16
Q

What does the oxygen dissociation curve show

A

Rate at which oxygen associated and dissociates with haemoglobin at different partial pressures of oxygen

17
Q

Whats the partial pressure of oxygen meanign

A

Partial pressure of O2 refers to the pressure exerted by oxygen within a mixture of gases, a measure of oxygen concentration

18
Q

What occues to O2 when haemoglobin has a higher affinity for oxygen

A

Haemoglobin can bind easily and dissociate slowly

19
Q

Which way does the curve move for high and low CO2 affinity

A

High affinity = right
Low affinity = left

20
Q

When is oxygen associated and where

A

Gas exchange surface
When O2 conc is high, CO2 conc is low and affinity of haemoglobin for O2 is high

21
Q

When is oxygen dissociated and where

A

Repiring tissues
When O2 conc is low, CO2 conc high, and affinity of haemoglobin for O2 is low

22
Q

Where does loading/ associating take place

A

In lungs

23
Q

Where does unloading and dissociating take palce

A

Tissues

24
Q

WHen do haemoglobins take up more O2 easily

A

Haemoglobin with high affinity for O2 = load easily and release less easily

25
Q

Describe the quanternary structure of haemoglobin

A

Four polypeptides are linked to form a spherical molecule
Each polyppetide is associated with a haem group which contains Fe2+ and can combine with a single O2

26
Q

How can substance X benefit endurance for athletes

A

Results in more red blood cells which means athletes have more haemoglobin
So more oxygen can be offloaded and absorbed
More ATP is released and used for muscle contraction
Delays anaerobic respiration

27
Q

What structure protein is haemoglobin

A

Quaternary with four polypeptide chains two alpha globins and two beta globins, each with a prosthetic haem group

28
Q

How are the four globin subunits held together

A

Disulphide bonds arranges with hydrophobic R group inwards and hydrophilic outwards

29
Q

What does the prosthetic haem contain

A

Iron II ion (Fe2+)

30
Q

Haemoglobins functions

A

-Oxygen binding and transporting
-Oxygen is insoluble in water but haemoglobin is soluble so can be caried efficiently
-Haem enables small molecueles to be bound more easily because each oxygen binds alters quaternary structure so other oxygen has higher chance of binding
-Iron II ion allows O2 to reversible bind

31
Q

What two types of globin proteins make up the haem group

A

Two alpha globins and two beta globins

32
Q

What is haemoglobins functions

A

1) binding O2 in lungs and transporting it to tissue for aerobic metabolic pathways
2) O2 not soluble inwater and haemoglobin is, O2 canbe carried more efficiently around the body
3) Existence of Fe2+ alows O2 to be reversible bind as amino acids arent well suited

33
Q

WHat happens if haemoglobin decreases in the bloodq

A

Fewer haemoglobin so less O2 is delivered o muscles
Less O2 means reduces AEROBIC RESPIRATION
Which means less ATP available for muscle contraction, reducing muscle contraction

34
Q

Advantage of someone having less haemoglobin if haemoglobin has a lower affnity for O2

A

(Graph shifts right) so haemoglobin has a lower affinity
Haemoglobin dissociates MORE oxygen
So oxygen is available for use in aerobic respiration
Demand for ATP can be met at lower haemoglobin concentrations

35
Q

Roles of haemoglobin

A

1) transport oxygen to aerobic metabolic pathways
2) Removing CO2 from respiring tissues
3) Dissociating oxygen from haemoglobin at respiring tissues

36
Q

Advantage of having a low affinity for O2

A

Dissociates at tissues more easily
So can have a greater rate of respiration