Hemoprotein

[2] Hemeproteins probably evolved to incorporate the iron atom contained within the protoporphyrin IX ring of heme into proteins.

As it makes hemeproteins responsive to molecules that can bind divalent iron, this strategy has been maintained throughout evolution as it plays crucial physiological functions.

[3] Oxygen (O2), nitric oxide (NO), carbon monoxide (CO) and hydrogen sulfide (H2S) bind to the iron atom in heme proteins.

Once bound to the prosthetic heme groups, these molecules can modulate the activity/function of those hemeproteins, affording signal transduction.

Myoglobin and hemoglobin are globular proteins that serve to bind and deliver oxygen using a prosthetic group.

These globins dramatically improve the concentration of molecular oxygen that can be carried in the biological fluids of vertebrates and some invertebrates.

In vertebrates, oxygen is taken into the body by the tissues of the lungs, and passed to the red blood cells in the bloodstream where it's used in aerobic metabolic pathways.

[13] Catalases are hemoproteins responsible for the catalysis of converting hydrogen peroxide into water and oxygen.

Haloperoxidases involved in the innate immune system also contain a heme prosthetic group.

[31] Recent design attempts have focused on creating all-beta heme binding proteins, whose novel topology is very rare in nature.

Such designs include: Some methodologies attempt to incorporate cofactors into the hemoproteins who typically endure harsh conditions.

In order to incorporate a synthetic cofactor, what must first occur is the denaturing of the holoprotein to remove the heme.