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Heme D is the site for oxygen reduction to water of many types of bacteria at low oxygen tension. [24] Heme S is related to heme B by having a formyl group at position 2 in place of the 2-vinyl group. Heme S is found in the hemoglobin of a few species of marine worms.
Second, medical roots generally go together according to language, i.e., Greek prefixes occur with Greek suffixes and Latin prefixes with Latin suffixes. Although international scientific vocabulary is not stringent about segregating combining forms of different languages, it is advisable when coining new words not to mix different lingual roots.
Heme B or haem B (also known as protoheme IX) is the most abundant heme. [1] Hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B. The peroxidase family of enzymes also contain heme B. The COX-1 and COX-2 enzymes (cyclooxygenase) of recent fame, also contain heme B at one of two active sites.
The name hemoglobin (or haemoglobin) is derived from the words heme (or haem) and globin, reflecting the fact that each subunit of hemoglobin is a globular protein with an embedded heme group. Each heme group contains one iron atom, that can bind one oxygen molecule through ion-induced dipole forces.
Heme A (or haem A) is a heme, a coordination complex consisting of a macrocyclic ligand called a porphyrin, chelating an iron atom. Heme A is a biomolecule and is produced naturally by many organisms. Heme A, often appears a dichroic green/red when in solution, is a structural relative of heme B, a component of hemoglobin, the red pigment in blood.
The main discussion of these abbreviations in the context of drug prescriptions and other medical prescriptions is at List of abbreviations used in medical prescriptions. Some of these abbreviations are best not used, as marked and explained here.
Heme is a major source of dietary iron in humans and other mammals, and its synthesis in the body is well understood, but heme pathways are not as well understood. It is likely that heme is tightly regulated for two reasons: the toxic nature of iron in cells, and the lack of a regulated excretory system for excess iron.
The average red blood cell contains 250 million hemoglobin molecules. [7] Hemoglobin contains a globin protein unit with four prosthetic heme groups (hence the name heme-o-globin); each heme is capable of reversibly binding with one gaseous molecule (oxygen, carbon monoxide, cyanide, etc.), [8] therefore a typical red blood cell may carry up to one billion gas molecules.