In binding of Hb and oxygen.oxyen unable to break the covalent bond between carbon monoxide and heme so,it is​ non competitive...so the answer is option (B)

Binding of Hemoglobin with Oxygen

The binding of hemoglobin (Hb) with oxygen is a crucial process in the transport of oxygen throughout the body. The interaction between Hb and oxygen can be categorized as follows:

Allosteric
- The binding of Hb with oxygen is allosteric in nature. Allosteric regulation involves the binding of a molecule at a site other than the active site, causing a conformational change in the protein structure.
- In the case of Hb, the binding of oxygen at one site induces a conformational change that increases the affinity of other subunits for oxygen. This cooperative binding allows Hb to efficiently pick up and release oxygen as needed.

Competitive vs. Non-Competitive
- The binding of Hb with oxygen is not competitive or non-competitive. Competitive inhibition occurs when a molecule competes with the substrate for the active site of the enzyme, which is not the case in the binding of Hb with oxygen.
- Non-competitive inhibition involves the binding of a molecule at a site other than the active site, altering the enzyme's activity. This type of inhibition is also not applicable to the binding of Hb with oxygen.

Irreversible
- The binding of Hb with oxygen is reversible. Oxygen molecules can bind to Hb in the lungs to form oxyhemoglobin and are then released in tissues to be utilized for cellular respiration.
- The reversible nature of this binding allows for efficient oxygen transport and delivery throughout the body to meet the metabolic demands of tissues.

In conclusion, the binding of Hb with oxygen is an allosteric, reversible process that allows for efficient oxygen transport and delivery in the body.