Heme O

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title: "Heme O" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["tetrapyrroles", "biomolecules"] topic_path: "general/tetrapyrroles" source: "https://en.wikipedia.org/wiki/Heme_O" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

| Verifiedfields = changed | Watchedfields = changed | verifiedrevid = 442001779 | ImageFile = Heme o structure.svg | ImageSize = | IUPACName = Iron(II) 3-[18-(2-carboxyethyl)-7-ethenyl-12-[(4E,8E)-1-hydroxy-5,9,13-trimethyltetradeca-4,8,12-trienyl]-3,8,13,17-tetramethylporphyrin-21,23-diid-2-yl]propanoic acid | OtherNames = | Section1 = {{Chembox Identifiers | CASNo_Ref = | CASNo = 137397-56-9 | PubChem = 15719509 | ChemSpiderID_Ref = | ChemSpiderID = 3571849 | SMILES = OC(=O)CC/c6c(\C)c3n7c6cc2c(/CCC(O)=O)c(/C)c1cc5n8c(cc4n([Fe]78n12)c(c=3)c(C=C)c4c)c(\C(O)CC\C=C(/C)CC\C=C(/C)CC\C=C(C)/C)c5\C | StdInChI_Ref = | StdInChI = 1S/C49H60N4O5.Fe/c1-10-35-31(6)40-26-45-49(46(54)19-13-18-30(5)17-12-16-29(4)15-11-14-28(2)3)34(9)41(53-45)24-38-32(7)36(20-22-47(55)56)43(51-38)27-44-37(21-23-48(57)58)33(8)39(52-44)25-42(35)50-40;/h10,14,16,18,24-27,46,54H,1,11-13,15,17,19-23H2,2-9H3,(H4,50,51,52,53,55,56,57,58);/q;+2/p-2/b29-16+,30-18+,38-24-,39-25-,40-26-,41-24-,42-25-,43-27-,44-27-,45-26-; | StdInChIKey_Ref = | StdInChIKey = FISPASSVCDRERW-KVGORYHISA-L | MeSHName = heme+O | Section2 = {{Chembox Properties | Formula = C49H58O5N4Fe | MolarMass = 838.854 g/mol | Appearance = | Density = | MeltingPt = | BoilingPt = | Section3 = {{Chembox Hazards | MainHazards = | FlashPt = | AutoignitionPt =

Heme O (or haem O) differs from the closely related heme A by having a methyl group at ring position 8 instead of the formyl group. The isoprenoid chain at position 2 is the same.

Heme O, found in the bacterium Escherichia coli, functions in a similar manner to heme A in mammalian oxygen reduction.

References

References

  1. (2004). "The Nature of the Exchange Coupling between High-Spin Fe(III) Heme o3 and CuB(II) in Escherichia coli Quinol Oxidase, Cytochrome bo3: MCD and EPR Studies". J. Am. Chem. Soc..

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tetrapyrrolesbiomolecules