Heme B

Heme B or haem B (also known as protoheme IX) is the most abundant heme, both 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.

Generally, heme B is attached to the surrounding protein matrix (known as the apoprotein) through a single coordination bond between the heme iron and an amino-acid side-chain.

Both hemoglobin and myoglobin have a coordination bond to an evolutionarily-conserved histidine, while nitric oxide synthase and cytochrome P450 have a coordination bond to an evolutionarily-conserved cysteine bound to the iron center of heme B.

Since the iron in heme B containing proteins is bound to the four nitrogens of the porphyrin (forming a plane) and a single electron donating atom of the protein, the iron is often in a pentacoordinate state. When oxygen or the toxic carbon monoxide is bound the iron becomes hexacoordinated.

Heme

Heme (from the Greek "Αίμα" which means blood) is a cofactor consisting of an Fe²⁺ (ferrous) ion contained in the centre of a large heterocyclic organic ring called a porphyrin, made up of four pyrrolic groups joined together by methine bridges. Not all porphyrins contain iron, but a substantial fraction of porphyrin-containing metalloproteins have heme as their prosthetic group; these are known as hemoproteins. Hemes are most commonly recognized as components of hemoglobin, the red pigment in blood, but are also found in a number of other biologically important hemoproteins such as myoglobin, cytochrome, catalase, heme peroxidase, and endothelial nitric oxide synthase.

Function

Hemoproteins have diverse biological functions including the transportation of diatomic gases, chemical catalysis, diatomic gas detection, and electron transfer. The heme ion serves as a source or sink of electrons during electron transfer or redox chemistry. In peroxidase reactions, the porphyrin molecule also serves as an electron source. In the transportation or detection of diatomic gases, the gas binds to the heme ion. During the detection of diatomic gases, the binding of the gas ligand to the heme ion induces conformational changes in the surrounding protein.