Globin and Protein Function Model
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Questions and Answers

What is the primary function of oxygen transport systems in large animals?

  • To allow for the transport of dissolved gas alone
  • To enable the circulation of respiratory molecules
  • To facilitate the pickup and release of oxygen at different locations (correct)
  • To provide respiratory molecules and cells for transport and storage

What is the key prosthetic group that allows globin proteins to bind oxygen?

  • The distal histidine residue
  • The ferrous (Fe2+) oxidation state of the iron atom
  • The porphyrin ring with a central metal atom (correct)
  • The proximal histidine residue

How does the iron atom in the heme group interact with oxygen?

  • The iron atom temporarily accepts an electron from oxygen, forming a superoxide radical (correct)
  • The iron atom is oxidized to the ferric (Fe3+) state, which prevents oxygen binding
  • The iron atom binds oxygen directly, forming a stable complex
  • The distal histidine residue forms a hydrogen bond with the oxygen molecule

What is the role of the proximal and distal histidine residues in the heme pocket?

<p>The proximal histidine binds the iron atom, while the distal histidine stabilizes the oxygen binding (B)</p> Signup and view all the answers

What is the significance of the Bohr effect in the regulation of hemoglobin?

<p>It decreases the affinity of hemoglobin for oxygen at low pH (C)</p> Signup and view all the answers

How does fetal hemoglobin differ from adult hemoglobin in its oxygen-binding properties?

<p>Fetal hemoglobin has a higher affinity for oxygen, allowing it to obtain oxygen from the mother's bloodstream (C)</p> Signup and view all the answers

What is the role of distal histidine in hemoglobin?

<p>It inhibits methemoglobin formation. (C)</p> Signup and view all the answers

How does hemoglobin enhance selectivity for oxygen?

<p>By preventing the release of toxic superoxide. (C)</p> Signup and view all the answers

How do myoglobin (Mb) and hemoglobin (Hb) differ?

<p>Hb is a monomer, while Mb is a tetramer. (A)</p> Signup and view all the answers

What effect does oxygen binding have on the magnetic properties of iron in hemoglobin?

<p>The iron becomes paramagnetic upon O2 binding. (A)</p> Signup and view all the answers

What happens to the Fe ion when oxygen binds to hemoglobin?

<p>Fe ion increases its oxidation state. (C)</p> Signup and view all the answers

In a simple binding reaction, what determines the equilibrium between P + L and PL?

<p>[P], [L], rate constants, and temperature. (A)</p> Signup and view all the answers

What structural change occurs in hemoglobin when oxygen binds?

<p>The alpha helix shifts slightly, altering the alpha-beta interface (D)</p> Signup and view all the answers

Why is the affinity of hemoglobin for oxygen lower in red blood cells compared to in vitro conditions?

<p>The presence of 2,3-bisphosphoglycerate (2,3-BPG) in red blood cells (D)</p> Signup and view all the answers

What is the primary function of 2,3-bisphosphoglycerate (2,3-BPG) in regulating hemoglobin activity?

<p>It stabilizes the T (tense) state of hemoglobin, decreasing oxygen affinity (C)</p> Signup and view all the answers

How does fetal hemoglobin differ from adult hemoglobin?

<p>It consists of alpha and gamma globin chains instead of alpha and beta (A)</p> Signup and view all the answers

What is the significant change in fetal hemoglobin that affects its interaction with 2,3-BPG?

<p>The histidine at position 143 is replaced by serine (A)</p> Signup and view all the answers

What is the Bohr effect in relation to hemoglobin?

<p>The decrease in hemoglobin's affinity for oxygen at lower pH (A)</p> Signup and view all the answers

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