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Heme 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chain at ring position 8 is oxidized into a formyl group, and one of the vinyl side chains, at ring position 2, has been replaced by an isoprenoid chain.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.
Additional recommended knowledge
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.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Heme_a". A list of authors is available in Wikipedia.|