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
does heme have a higher affinity for CO or O2?
CO
what are the characteristics of myoglobin and its function
high affinity for O2
role: stores O2, and releases during crisis involving O2 deprivation
what is the structure of hemoglobin
a tetramer of two subunits; alpha and beta
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