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Heme (American English), or haem (Commonwealth English, both pronounced /hi:m/ HEEM), is a ring-shaped iron-containing molecular component of hemoglobin, which is necessary to bind oxygen in the bloodstream. It is composed of four pyrrole rings with 2 vinyl and 2 propionic acid side chains. [1] Heme is biosynthesized in both the bone marrow and ...
A hemeprotein (or haemprotein; also hemoprotein or haemoprotein), or heme protein, is a protein that contains a heme prosthetic group. [1] They are a very large class of metalloproteins . The heme group confers functionality, which can include oxygen carrying , oxygen reduction, electron transfer, and other processes.
Hemerythrin does not, as the name might suggest, contain a heme. The names of the blood oxygen transporters hemoglobin, hemocyanin, and hemerythrin do not refer to the heme group (only found in globins). Instead, these names are derived from the Greek word for blood.
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.
The ultra-violet (UV) to visible spectroscopic signatures of hemes are still used to identify heme type from the reduced bis-pyridine-ligated state, i.e., the pyridine hemochrome method. Within each class, cytochrome a , b , or c , early cytochromes are numbered consecutively, e.g. cyt c , cyt c 1 , and cyt c 2 , with more recent examples ...
Example(s) bacillus: rod-shaped Latin baculus, stick Bacillus anthracis: bacteri-Pertaining to bacteria: Latin bacterium; Greek βακτήριον (baktḗrion), small staff bacteriophage, bactericide: balan-of the glans penis or glans clitoridis: Greek βάλανος (bálanos), acorn, glans balanitis: bas-of or pertaining to base
The number of heme C units bound to a holoprotein is highly variable. For vertebrate cells one heme C per protein is the rule but for bacteria this number is often 2, 4, 5, 6 or even 16 heme C groups per holoprotein. It is generally agreed the number and arrangement of heme C groups are related and even required for proper holoprotein function.
Like hemoglobin, myoglobin is a cytoplasmic protein that binds oxygen on a heme group. It harbors only one globulin group, whereas hemoglobin has four. Although its heme group is identical to those in Hb, Mb has a higher affinity for oxygen than does hemoglobin but fewer total oxygen-storage capacities. [22]