A single gene 'invented' hemoglobin several times

Thanks to the marine worm Platynereis dumerilii, an animal whose genes have evolved very slowly, scientists from CNRS, Université de Paris and Sorbonne Université, in association with others at the University of Saint Petersburg ...

How Archaea might find their food

The microorganism Methanosarcina acetivorans lives off everything it can metabolize into methane. How it finds its sources of energy, is not yet clear. Scientists at the Ruhr-Universität Bochum together with colleagues from ...

Japan aquarium shows mysterious clear-blood fish

The deep oceans have yielded many mysteries that have puzzled people for centuries, from the giant squid to huge jellyfish that look like UFOs. To that list add a fish with totally transparent blood.

Resurrected mammoth blood very cool (w/ Video)

(PhysOrg.com) -- A team of international researchers has brought the primary component of mammoth blood back to life using ancient DNA preserved in bones from Siberian specimens 25,000 to 43,000 years old.


Hemoglobin (English pronunciation: /hiːməˈɡloʊbɪn/; also rendered as haemoglobin and abbreviated Hb or Hgb) is the iron-containing oxygen-transport metalloprotein in the red blood cells of all vertebrates, with the exception of the fish family Channichthyidae, as well as the tissues of some invertebrates. Hemoglobin in the blood carries oxygen from the respiratory organs (lungs or gills) to the rest of the body (i.e., the tissues) where it releases the oxygen to burn nutrients to provide energy to power the functions of the organism, and collects the resultant carbon dioxide to bring it back to the respiratory organs to be dispensed from the organism.

In mammals, the protein makes up about 97% of the red blood cells' dry content, and around 35% of the total content (including water).[citation needed] Hemoglobin has an oxygen binding capacity of 1.34 ml O2 per gram of hemoglobin, which increases the total blood oxygen capacity seventy-fold compared to dissolved oxygen in blood. The mammalian hemoglobin molecule can bind (carry) up to four oxygen molecules.

Hemoglobin is involved in the transport of other gases: it carries some of the body's respiratory carbon dioxide (about 10% of the total) as carbaminohemoglobin, in which CO2 is bound to the globin protein. The molecule also carries the important regulatory molecule nitric oxide bound to a globin protein thiol group, releasing it at the same time as oxygen.

Hemoglobin is also found outside red blood cells and their progenitor lines. Other cells that contain hemoglobin include the A9 dopaminergic neurons in the substantia nigra, macrophages, alveolar cells, and mesangial cells in the kidney. In these tissues, hemoglobin has a non-oxygen-carrying function as an antioxidant and a regulator of iron metabolism.

Hemoglobin and hemoglobin-like molecules are also found in many invertebrates, fungi, and plants. In these organisms, hemoglobins may carry oxygen, or they may act to transport and regulate other things such as carbon dioxide, nitric oxide, hydrogen sulfide and sulfide. A variant of the molecule, called leghemoglobin, is used to scavenge oxygen, to keep it from poisoning anaerobic systems, such as nitrogen-fixing nodules of leguminous plants.

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