|Molar mass||684.64904 g/mol|
|Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)|
Heme C (or haem C) is an important kind of heme.
The correct structure of heme C was published, in mid 20th century, by the Swedish biochemist K.-G. Paul. This work confirmed the structure first inferred by the great Swedish biochemist Hugo Theorell. The structure of heme C, based upon NMR and IR experiments of the reduced, Fe(II), form of the heme, was confirmed in 1975. The structure of heme C including the absolute stereochemical configuration about the thioether bonds was first presented for the vertebrate protein and is now extended to many other heme C containing proteins.
Heme C differs from heme B in that the two vinyl side chains of heme B are replaced by covalent, thioether linkages to the apoprotein. Note that the two thiol groups are typically donated from the cysteine residues of the protein, and thus the net additional molecular weight of heme c as it is incorporated into the holoprotein, with the loss of two hydrogen atoms to form the bond, is 616.5 Da. These linkages do not allow the heme C to easily dissociate from the holoprotein, cytochrome c, compared with the more easily dissociated heme B that may dissociate from the holoprotein, the heme-protein complex, even under mild conditions. This allows a very wide range of cytochrome c structure and function, with the myriad of c type cytochromes acting primarily as electron carriers.
The thioether linkages seem to allow a great freedom of function for the holoproteins. In general, the c type cytochromes can be "fine tuned" over a wider range of oxidation-reduction potential than cytochromes b. This may be an important reason why cytochrome c is nearly ubiquitous throughout life. Heme C also plays an important role in apoptosis where just a few molecules of cytoplasmic cytochrome c, which must still contain heme C, leads to programmed cell death.
In addition to these equatorial covalent bonds, the heme iron is also usually axially coordinated to the side chains of two amino acids, making the iron hexacoordinate. For example, mammalian and tuna cytochrome c contain a single heme C that is axially coordinated to side chains of both histidine and methionine. Perhaps because of the two covalent bonds holding the heme to the protein, the iron of heme C is sometimes axially ligated to the amino group of lysine or even water.
- Paul, K.G.; Högfeldt, Erik; Sillén, Lars Gunnar; Kinell, Per-Olof (1950). "The splitting with silver salts of the cysteine-porphyrin bonds in cytochrome c". Acta Chemica Scandinavica 4: 239–244.
- Caughey, W.S. et al. (1975). "Heme A of Cytochrome c Oxidase".
- Takano T., Trus B.L., Mandel N., Mandel G., Kallai O.B., Swanson R., Dickerson R.E. (1977). "Tuna cytochrome c at 2.0 A resolution. II. Ferrocytochrome structure analysis.".
- Diode or Tunnel-Diode Characteristics? Resolving the Catalytic Consequences of Proton Coupled Electron Transfer in a Multi-Centered Oxidoreductase
- Bowman, S.E.J., Bren, K.L. (2008). "The chemistry and biochemistry of heme C: functional bases for covalent attachment". Nat. Prod. Rep. 25 (6): 1118–1130.
- Yeh, S.R., Han, S., and Rousseau, D.L. (1998). "Cytochrome c folding and unfolding". Accounts of Chemical Research 31 (11): 727–735.