Heme O
Identifiers
3D model (JSmol)
ChemSpider
MeSH heme+O
  • InChI=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-; ☒N
    Key: FISPASSVCDRERW-KVGORYHISA-L ☒N
  • 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
Properties
C49H58O5N4Fe
Molar mass 838.854 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Infobox references

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,[1] functions in a similar manner to heme A in mammalian oxygen reduction.

See also

References

  1. ↑ Myles R. Cheesman; Vasily S. Oganesyan; Nicholas J. Watmough; Clive S. Butler; Andrew J. Thomson (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. 126 (13): 4157–4166. doi:10.1021/ja038858m. PMID 15053605.
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