Heme c
From Wikipedia, the free encyclopedia
| Heme c | |
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| Identifiers | |
| CAS number | [] |
| PubChem | |
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| Properties | |
| Molecular formula | C34H36O4N4S2Fe |
| Molar mass | 684.651 g/mol |
| Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa) Infobox disclaimer and references |
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Heme C differs from heme B in that the two vinyl side chains are covalently bound to the apoprotein itself through thioether linkages.
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 hemeproteins, 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.
[edit] References
- ^ Yeh, S.R., Han, S., and Rousseau, D.L. (1998). "Cytochrome c folding and unfolding". Accounts of Chemical Research 31 (11): 727-735.
