Hemocyanin vs. Hemoglobin — What's the Difference?

A respiratory protein using copper to bind oxygen, turning blue when oxygenated.

Found exclusively within red blood cells.

Does not bind to cells but floats freely.

Widely studied for its role in many diseases.

Evolved independently of hemoglobin.

Gives blood its characteristic red color when oxygenated.

Found in many mollusks and arthropods.

Efficient in oxygen transport, especially under varying oxygen levels.

More efficient in cold temperatures.

An iron-containing protein in red blood cells, essential for oxygen transport in vertebrates.

Hemocyanins (also spelled haemocyanins and abbreviated Hc) are proteins that transport oxygen throughout the bodies of some invertebrate animals. These metalloproteins contain two copper atoms that reversibly bind a single oxygen molecule (O2).

Hemoglobin, or haemoglobin (spelling differences) (from Greek αἷμα, haîma 'blood' + Latin globus 'ball, sphere' + -in) (), abbreviated Hb or Hgb, is the iron-containing oxygen-transport metalloprotein in the red blood cells (erythrocytes) of almost all vertebrates (the exception being the fish family Channichthyidae) as well as the tissues of some invertebrates. Hemoglobin in blood carries oxygen from the lungs or gills to the rest of the body (i.e.

A bluish, copper-containing protein with an oxygen-carrying function similar to that of hemoglobin, present in the circulatory system of certain mollusks and arthropods.

The protein in the red blood cells of vertebrates that carries oxygen from the lungs to tissues and that consists of four polypeptide subunits, each of which is bound to an iron-containing heme molecule.

(biochemistry) a blue copper-containing respiratory pigment (a metalloprotein) found in most molluscs, and some arthropods

(American spelling) The iron-containing substance in red blood cells that transports oxygen from the lungs to the rest of the body; it consists of a protein (globulin), and haem (a porphyrin ring with an atom of iron at its centre).

The normal coloring matter of the red blood corpuscles of vertebrate animals. It is composed of hematin and globulin, and is also called hæmatoglobulin. In arterial blood, it is always combined with oxygen, and is then called oxyhemoglobin. It crystallizes under different forms from different animals, and when crystallized, is called hæmatocrystallin. See Blood crystal, under Blood.

A hemoprotein composed of globin and heme that gives red blood cells their characteristic color; function primarily to transport oxygen from the lungs to the body tissues;

No, humans and all other vertebrates use hemoglobin, not hemocyanin.

Hemoglobin is generally more efficient, especially under conditions of low oxygen pressure.

Understanding these proteins helps in studying evolutionary biology, respiratory physiology, and developing treatments for related diseases.

Hemocyanin uses copper for oxygen transport and is blue when oxygenated, while hemoglobin uses iron and turns red.

Hemocyanin is more suited to stable, cold, and low-oxygen environments, common in marine settings where these animals typically live.

Hemocyanin functions better at colder temperatures, while hemoglobin is adapted to a wider range of temperatures, including those found in human environments.

While primarily of interest in comparative physiology and evolutionary studies, research into hemocyanin's properties could inspire biomedical applications.

The presence of hemocyanin or hemoglobin affects the color of an organism's blood—blue or red, respectively.

They illustrate different evolutionary solutions to the problem of oxygen transport, reflecting adaptations to various ecological niches.

Synthetic analogs have been developed for research and medical applications, especially for hemoglobin.