Heme c

Heme C differs from heme B in that the two vinyl side chains are covalently bound to the apoprotein itself through thioether linkages.

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In addition to these covalent bonds, the heme iron is also usually coordinated to two side chains of amino acids, making the iron hexacoordinate. For example, cytochrome c contains a single heme C that is coordinated to side chains of both histidine and methionine.^[1] bc₁ complex is another protein that contains a C type heme.

Some hemoproteins, often from single cell organisms, may contain up to four hemes C.

The correct structure of heme C was first published, in mid 20th century, by the Swedish biochemist K.-G. Paul.

See also

• Heme

References

1. ^ Yeh, S.R., Han, S., and Rousseau, D.L. (1998). "Cytochrome c folding and unfolding". Accounts of Chemical Research 31 (11): 727-735.