3.3 Chapter 7- Mass Transport Flashcards
Give the key features of haemoglobin.
Many organisms have haemoglobin to transport oxygen and the type varies depending on their needs. Haemoglobin is highly adapted for transporting oxygen.
Describe the structure of haemoglobin.
- Group of chemically similar molecules found in many different organisms.
- Large proteins with a quanternary structure of four polypeptide chains
- Evolved to be efficient at loading oxygen in certain conditions and unloading it in others.
- Primary structure- the sequence of amino acids in the 4 polypeptide chains.
- Secondary structure- polypeptide chains coiled into a helix.
- Tertiary structure- haemoglobin folded into a precise shape to carry oxygen.
- Quanternary structure- four peptide chains linked together- each one associated with a haem group - iron ion of Fe2+- gives the haemoglobin its red colour- can combine with oxygen to form Fe3+ so 4 oxygen can be carried by a single human haemoglobin.
Describe briefly how oxygen and haemoglobin interact.
- Oxygen joins to haemoglobin in red blood cells to form oxyhemoglobin.
- Reversible reaction.
- Oxygen leaves near body cells.
Describe the key terms surrounding the action of haemoglobin and where these terms occur.
- Binding oxygen= loading/ association- occurs in human lungs
- Releasing oxygen= dissociation/ unloading- occurs in human tissue.
Why is haemoglobin important for the circulatory system?
- An important part of the circulatory system.
- Found in human red blood cells.
- Red blood cells and haemoglobin have a role of transporting oxygen around the body.
What is important about haemoglobin in different organisms?
- Many chemically similar types of haemoglobin in different organisms carry out the same function.
- Haemoglobin is found in many organisms from vertebrates to humans.
What does affinity mean in terms of haemoglobin (define affinity)?
- Affinity is the tendency for a molecule to bind with oxygen.
- Haemoglobin’s affinity varies depending on its conditions.
- Haemoglobin with a higher affinity for oxygen takes it up more easily, but releases it less easily and vice versa.
What role does haemoglobin have and what features mechanics does it have to achieve this?
- To be efficient at transporting oxygen haemoglobin has to readily associate with oxygen where gas exchange occurs and readily dissociate from oxygen at tissues.
- Does this by changing its affinity for oxygen at different conditions.
- Shape changes in the presence of e.g. CO2- binds more loosely with oxygen and releases oxygen more easily.
What is the oxygen disassociation curve? Draw it and explain.
- The graph of the saturation of haemoglobin with the partial pressure of oxygen.
- Affinity affects how saturated haemoglobin is.
- pO2 is high- e.g. the lungs- oxygen affinity increases- oxygen saturation increases.
- pO2 is low- e.g. respiring tissues- oxygen affinity decreases- oxygen saturation decreases.
- Saturation of haemoglobin affects affinity and shape, so the graph is S-shaped not a straight line.
How does hemoglobin’s affinity vary with regards to pO2?
- Haemoglobin’s affinity varies depending on the partial pressure of oxygen- pO2= measure of oxygen concentration.
- More oxygen = more pO2 = more affinity for oxygen.
- Areas of high pO2- oxygen loads onto haemoglobin to form oxyhaemoglobin
- Areas of low pO2- oxyhemoglobin unloads oxygen.
- Oxygen enters the blood at the alveoli in the lungs with a high pO2 so oxyhemoglobin is formed.
- Cells aerobically respire- use up oxygen- lower the pO2- oxyhaemoglobin in red blood cells unloads oxygen and haemoglobin returns to the lungs.
What happens at different partial pressures with haemoglobin?
At different partial pressures of oxygen haemoglobin loads, transports and unloads oxygen.
Describe step by step the oxyhaemoglobin dissociation curve and draw it.
Hint: 3 Steps
- The first haemoglobin finds it more difficult to bind as its 4 sites are close together. At a low PO2 (oxygen concentration) little oxygen binds.
- First O2 molecule associating- changes the quanternary structure of the haemoglobin- shape change uncovers second binding site- easier for oxygen to bind. Binding of the 1st molecule helps other molecules- takes a smaller pO2 increase to bind to the 2nd oxygen- positive cooperativity/ cooperative binding- makes it easier to bind to the 2nd molecule- steeper curve- small change in pO2 = more oxygen loading.
- Third molecule binds to haemoglobin- harder for oxygen to bind- less likely to find an empty site- gradient of the graph reduces and flattens.
Why does the shape of oxygen dissociation curves vary?
- Shape of the haemoglobin can change under certain conditions and/or between species.
- A wide variety of oxygen dissociation curves
What does an oxyhemoglobin curve moving left or right mean?
- Further to the left= greater affinity- haemoglobin loads oxygen easily but doesn’t find it easily easy to unload.
- Further to right = lower affinity.
Describe and name the effect of CO2 on haemoglobin include. the effect on the oxygen dissociation curve.
- The partial pressure of carbon dioxide- pCO2- a measure of CO2 concentration.
- Greater pCO2 produces acid due to the dissolving of CO2- decreases the pH- causes haemoglobin to change shape and release oxygen- dissociate.
- Haemoglobin- reduced affinity for oxygen in the presence of high pCO2= increased oxygen- the Bohr effect.
- Helps haemoglobin release more oxygen at times of high activity
- Increases oxygen association at the lungs- CO2 concentration low as it diffuses across the exchange surface and is excreted- affinity of oxygen increases- the loading of oxygen increases- oxygen dissociation curves shifts to the left.
- Respiring tissues- increased pCO2 decreases oxygen affinity- low pO2 and high pCO2- oxygen is readily unloaded to muscle cells- the oxygen dissociation curve is shifted to the right.
Why is the effect of CO2 on haemoglobin in organisms important?
- The effects of CO2 on haemoglobin helps haemoglobin release more oxygen in times of high activity.
- The Bohr effect increases dissociation of oxygen for aerobic respiration at the tissues in times of high activity.
Why might pCO2 per breath not change during intense exercise?
During periods of high exercise, pCO2 may not change per breath as breathing rate or tidal volume may increase instead.
Describe the gas exchange process of haemoglobin.
(Hint: 5 steps)
- At gas exchange surfaces CO2 is constantly removed.
- pH increases due to low concentration of CO2.
- Increased pH causes haemoglobin to change shape, making it have a higher affinity and more easily load oxygen.
- High affinity means the oxygen isn’t released while it’s being transported. CO2 is produced in the tissues and is acidic in solution- the pH in the blood around the tissues decreases.
- Changes the shape- quanternary structure- of the haemoglobin to have a lower affinity- increases oxygen dissociation.
- Haemoglobin releases oxygen into respiring tissues.
How does the gas exchange process change? And why is this important?
- Process is flexible to ensure there is always sufficient oxygen for respiring tissues.
- The more active the organism= more respiration occurs= higher pCO2 = lower pH= more haemoglobins shape changes= more oxygen is unloaded = more O2 is released for respiration.
- This ensures in times of high activity more oxygen reaches respiring cells for aerobic respiration to produce ATP.
Why is not all haemoglobin saturated and describe the saturation of haemoglobin at different stages?
- In humans haemoglobin is a saturated the lungs
- Not all is saturated as atmospheric pressure is usually 97%.
- When haemoglobin reaches a tissue with a low respiratory rate- 1 oxygen molecule is released, but blood is still 75% saturated with oxygen when it reaches the lungs.
- In high respiratory rates- 3 oxygen molecules are released.
What are the features of different haemoglobins in different organisms
- All haemoglobins are chemically similar and found in many different organisms.
- Slight differences between different organisms.
- Different types of haemoglobin within/ between species have different dissociation curves.
- Found in some vertebrates, worms, some insects and some bacteria.
Why are there different types of haemoglobin?
- Different types of haemoglobin with different oxygen transporting capacities and properties relating to the different organisms living conditions
What causes haemoglobin to have different properties and what are these properties?
- Different carrying capacity is related to the shape of the haemoglobin.
- Each organism has a haemoglobin with a slightly different amino acid sequence, so a different quanternary structure, binding capacity and affinity.
What determines the type of haemoglobin and organism has?
- The different types of haemoglobin are evolved adaptions related to an organism’s habitat, environment, size and activity to help it survive.
- e.g. A low pO2 environment= higher affinity haemoglobin.