Heme C

Source: Wikipedia, the free encyclopedia.
Heme C
Identifiers
3D model (
JSmol
)
ChemSpider
MeSH heme+C
  • InChI=1S/C34H34N4O4S2.Fe/c1-15-21(7-9-31(39)40)27-14-28-22(8-10-32(41)42)16(2)24(36-28)12-29-34(20(6)44)18(4)26(38-29)13-30-33(19(5)43)17(3)25(37-30)11-23(15)35-27;/h11-14H,5-10H2,1-4H3,(H6,35,36,37,38,39,40,41,42,43,44);/q;+2/p-2/b23-11-,24-12-,25-11-,26-13-,27-14-,28-14-,29-12-,30-13-; ☒N
    Key: KWLVFEFHZOXGTI-IDTMDVKXSA-L ☒N
  • OC(=O)CC/c6c(\C)c3n7c6cc2c(/CCC(O)=O)c(/C)c1cc5n8c(cc4n([Fe]78n12)c(c=3)c(C(S)=C)c4c)c(\C(S)=C)c5\C
Properties
C34H36O4N4S2Fe
Molar mass 684.64904 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
☒N verify (what is checkY☒N ?)

Heme C (or haem C) is an important kind of heme.

History

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

stereochemical configuration about the thioether bonds was first presented for the vertebrate protein, cytochrome c[3]
and is now extended to many other heme C containing proteins.

Properties

Heme C differs from

cytochromes acting primarily as electron carriers. The redox potential for cytochrome c can also be "fine-tuned" by small changes in protein structure and solvent interaction.[4]

The number of heme C units bound to a

bc1 complex
is another important enzyme that contains a C type heme.

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.[6] Cytochrome c can be measured in human serum and can be used as a marker for inflammation.[7]

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.[8] 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.

See also

References

  1. doi:10.3891/acta.chem.scand.04-0239
    .
  2. PMID 170266
    .
  3. PMID 188826
    .
  4. PMID 1311391
    .
  5. PMID 16248601.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  6. PMID 19030605.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
  7. PMID 27489552
    .
  8. doi:10.1021/ar970084p.{{cite journal}}: CS1 maint: multiple names: authors list (link
    )
Retrieved from "https://en.wikipedia.org/w/index.php?title=Heme_C&oldid=1185453285"
This page is based on the copyrighted Wikipedia article: Heme C. Articles is available under the CC BY-SA 3.0 license; additional terms may apply.Privacy Policy