Because it is associated with cooperative oxygen binding. NONCOOPERATIVE VS. COOPERATIVE OXYGEN BINDING Noncooperative oxygen binding is commonly associated with myoglobin. It is a monomer. It has a hyperbolic oxygen binding curve and does NOT have cooperative oxygen binding. This is described as: ##Y_(O_2) = (P_(O_2))/(K_D + P_(O_2))## where ##Y## is the fractional saturation (y-axis) ##P_(O_2)## is the partial pressure of oxygen in ##torr## (x-axis) and ##K_D## is the dissociation constant for binding events. ##K_D## is smaller for higher binding affinities. Cooperative oxygen binding is basically an effect where oxygen binding affinity can change depending on how much oxygen is bound and this is described via a sigmoidal binding curve. HEMOGLOBIN Hemoglobin an ##alpha_2beta_2## heterotetramer is the prime example for sigmoidal oxygen binding curves. Its binding curve is defined as: ##Y_(O_2) = (P_(O_2)^n)/(P_50^n + P_(O_2)^n)## where ##Y## is the fractional saturation (y-axis) ##P_(O_2)## is the partial pressure of oxygen in ##torr## (x-axis) ##P_50## is the partial pressure of oxygen when ##K_D = P_(O_2)## and ##K_D## is the dissociation constant for binding events. ##n
Because it is associated with cooperative oxygen binding.
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