myoglobin/hemoglobin

  1. what is the structure of myoglobin
    • single chain, high a-helical content, globular
    • heme prosthetic group: iron Fe2+ ferrous,
  2. what are the 6 coordination sites in the heme prosthetic group
    • four site are occupied by nitrogen
    • fifth site occupied by nitrogen. from proximal histidine residue
    • sixth site occupied by oxygen/CO. from distal histidine
  3. does heme have a higher affinity for CO or O2?
    CO
  4. what are the characteristics of myoglobin and its function
    • high affinity for O2
    • role: stores O2, and releases during crisis involving O2 deprivation
  5. what is the structure of hemoglobin
    a tetramer of two subunits; alpha and beta
  6. explain the concept of cooperativity/cooperative binding
    when an O2 molecule binds to the first site, it causes a conformational change in the tetrameric structure of hemoglobin which increases the oxygen binding capacity of hemoglobin
Author
tanyalequang
ID
342622
Card Set
myoglobin/hemoglobin
Description
comparing structure and function of myoglobin and hemoglobin
Updated