Hemerythrin
| Hemerythrin HHE cation binding domain | |||||||||
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crystal structures of an antibody to a peptide and its complex with peptide antigen at 2.8 angstroms
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| Identifiers | |||||||||
| Symbol | Hemerythrin | ||||||||
| Pfam | PF01814 | ||||||||
| InterPro | IPR012312 | ||||||||
| PROSITE | PDOC00476 | ||||||||
| SCOP | 2hmq | ||||||||
| SUPERFAMILY | 2hmq | ||||||||
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| Available protein structures: | |
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| Pfam | structures |
| PDB | RCSB PDB; PDBe; PDBj |
| PDBsum | structure summary |
Hemerythrin (also spelled haemerythrin; from Greek words αίμα = blood and ερυθρός = red) is an oligomeric protein responsible for oxygen (O2) transport in the marine invertebrate phyla of sipunculids, priapulids, brachiopods, and in a single annelid worm genus, Magelona. Myohemerythrin is a monomeric O2-binding protein found in the muscles of marine invertebrates. Hemerythrin and myohemerythrin are essentially colorless when deoxygenated, but turn a violet-pink in the oxygenated state.
Hemerythrin does not, as the name might suggest, contain a heme. The names of the blood oxygen transporters hemoglobin, hemocyanin, hemerythrin, do not refer to the heme group (only found in globins), instead these names are derived from the Greek word for blood.Recent evidence has revealed hemerythrin to be a multi-functional protein – contributing to innate immunity and anterior tissue regeneration in worms.
The mechanism of dioxygen binding is unusual. Most O2 carriers operate via formation of dioxygen complexes, but hemerythrin holds the O2 as a hydroperoxide. The site that binds O2 consists of a pair of iron centres. The iron atoms are bound to the protein through the carboxylate side chains of a glutamate and aspartates as well as through five histidine residues. Hemerythrin and myohemerythrin are often described according to oxidation and ligation states of the iron centre:
The uptake of O2 by hemerythrin is accompanied by two-electron oxidation of the diferrous centre to produce a hydroperoxide (OOH−) complex. The binding of O2 is roughly described in this diagram:
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