Металлпротеиндер мен тыныс пигменттері

Metalloprotein
A respiratory pigment is a metalloprotein that serves a variety of important functions, its main being O2 transport. Other functions performed include O2 storage, CO2 transport, and transportation of substances other than respiratory gases. There are four major classifications of respiratory pigment: hemoglobin, hemocyanin, erythrocruorin–chlorocruorin, and hemerythrin. The heme containing globin is the most commonly occurring respiratory pigment, occurring in at least 9 different phyla of animals.

Vertebrates use a tetrameric hemoglobin, carried in red blood cells, to breathe. There are multiple types of hemoglobin that have been found in the human body alone. Hemoglobin A is the “normal” hemoglobin, the variant of hemoglobin that is most common after birth. Hemoglobin A2 is a minor component of hemoglobin found in red blood cells. Hemoglobin A2 makes up less than 3% of total red blood cell hemoglobin. Hemoglobin F typically is only found in the fetal stage of development. While Hemoglobin F falls dramatically after birth, it is possible for some people to produce some levels of Hemoglobin F throughout their full life.

Animals use a great variety of globins for respiration. By structure, they can be classified as:
Intracellular Hbs. These globins reside inside a cell, much like the vertebrate Hb. Multi subunit Hbs. These globins form complexes and work outside a cell. Multi domain, multisubunit Hbs. These globins form complexes, work outside a cell, and have multiple globin domains per peptide chain. Erythrocruorin and chlorocruorin belong to the multisubunit Hbs, specifically of the 12 dodecamer type.

Leghemoglobin is a molecular similar in structure to myoglobin that is currently being used in artificial meat products, such as the Impossible Burger, to simulate both the color and taste of meat. Similar in function to hemoglobin, leghemoglobin contains trace amounts of iron, but it is primarily found in plant roots.

Hemocyanin is a respiratory pigment that uses copper as its oxygen binding molecule, as opposed to iron with hemoglobin. Hemocyanin is found in both arthropods and Mollusca, however it is thought that the molecule independently evolved in both phyla. There are several other molecules that exist in arthropods and Mollusca that are similar in structure to hemocyanin but serve entirely different purposes. For example, there are copper containing tyrosinases that play significant roles in immune defense, wound healing, and the arthropod's cuticle. Molecules similar to hemocyanin in structure are grouped in under the hemocyanin superfamily.