Heme b
From Wikipedia, the free encyclopedia
| Heme b | |
|---|---|
 |
|
| Identifiers | |
| CAS number | [] |
| PubChem | |
| MeSH | |
| Properties | |
| Molecular formula | C34H34O4N4Fe |
| Molar mass | 616.487 |
| Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) Infobox disclaimer and references |
|
Heme B is the most abundant heme; both hemoglobin and myoglobin are examples of oxygen transport proteins that contain heme B and 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 evolutionary conserved histidine, while Nitric oxide synthase and Cytochrome P450 have a coordination bond to an evolutionary 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 bound with oxygen or the toxin carbon monoxide the iron is hexacoordinated.
