Respuesta :
The correct answer is option (A). Hemoglobin-oxygen binding affinity would dramatically decrease due to the prevention of cooperative binding.
Hemoglobin's essential function is to carry oxygen and Porphyrin rings are essential for that. For instance, when one of hemoglobin's four binding sites is occupied by an oxygen atom, the affinity of the remaining three binding sites for oxygen increases; as a result, oxygen is more likely to bind to hemoglobin that has been bound to oxygen than to unbound hemoglobin. Cooperative binding is the term used to describe this.
Our metabolizing tissues receive sufficient oxygen delivery and transport thanks to the cooperative binding.
For example, when an oxygen atom binds to one of hemoglobin's four binding sites, the affinity to the oxygen of the three remaining available binding sites increases; i.e. oxygen is more likely to bind to hemoglobin bound to one oxygen than to unbound hemoglobin which is called cooperative binding which ensures adequate oxygen transport and delivery to our metabolizing tissues.
The complete question is:
If this iron atom acted like typical coenzymes, which are loosely bound to their associated enzymes and can dissociate immediately after the catalyzed reaction, how would hemoglobin’s ability to transport oxygen be altered?
A. Hemoglobin-oxygen binding affinity would dramatically decrease due to the prevention of cooperative binding.
B. There would be no effect on hemoglobin’s binding affinity to oxygen because the iron typically falls off after O2 binds.
C. Hemoglobin-oxygen binding affinity would be reduced due to increased competition from protons and carbon monoxide.
D. Hemoglobin-oxygen binding affinity would increase due to reduced steric hindrance in the active site.
To learn more about Hemoglobin please click on the given link: https://brainly.com/question/28907203
#SPJ4
