Accession NumberHMDB06901
Common_NameHeme A
DescriptionHeme A differs from heme B in that a methyl side chain at ring position 8 is oxidized into a formyl group, and one of the vinyl side chains, at ring position 2, has been replaced by an isoprenoid chain. Like heme B, heme A is often attached to the apoprotein through a coordination bond between the heme iron and a conserved amino acid side-chain. An example of a metalloprotein that contains heme A is cytochrome c oxidase. Both the formyl group and the isoprenoid side chain are thought to play important roles in conservation of the energy of oxygen reduction by cytochrome c oxidase.(Wikipedia)
Chemical_IUPAC_NameNot Available
Chemical FormulaC49H56FeN4O6
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Predicted 1H NMR SpectrumDownload
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Predicted 13C NMR SpectrumDownload
Predicted 13C NMR PeaklistDownload
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