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Haemoglobin and the Bohr effect

  • 4 things to know
  • Papers 1, 2 and 3

Overview

Recall questions on the quaternary structure of haemoglobin and its haem groups, cooperative binding, the Bohr effect and its mechanism through carbonic acid and hydrogen ions, and the forms in which carbon dioxide is carried in the blood.

What you need to know

Answer each one before you reveal it.

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Key term

What is the Bohr effect, and how does it shift the oxygen dissociation curve?

Key term

How many polypeptide subunits make up a haemoglobin molecule?

Key term

What prosthetic group is found in each subunit of haemoglobin?

Key term

How many alpha chains are present in adult haemoglobin?

Questions from this subtopic

Each one with the model answer underneath.

  1. 1

    What type of protein structure does haemoglobin possess?

    Model answer

    Quaternary structure.

  2. 2

    How many polypeptide subunits make up a haemoglobin molecule?

    Model answer

    Four polypeptide subunits.

  3. 3

    What prosthetic group is found in each subunit of haemoglobin?

    Model answer

    A haem group.

  4. 4

    What ion is located at the centre of each haem group in haemoglobin?

    Model answer

    An iron(II) ion (Fe²⁺).

  5. 5

    What is the maximum number of oxygen molecules that one haemoglobin molecule can carry, and what is the resulting compound called?

    Model answer

    Four oxygen molecules; the compound formed is oxyhaemoglobin.

  6. 6

    In cooperative binding, what happens when the first oxygen molecule binds to haemoglobin?

    Model answer

    The first oxygen molecule binds to one of the haem groups.

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