Cofactor F430

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title: "Cofactor F430" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["tetrapyrroles", "cofactors", "nickel-compounds"] topic_path: "arts/film" source: "https://en.wikipedia.org/wiki/Cofactor_F430" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

| ImageFile=Coenzyme F430.svg | ImageSize=220px | IUPACName= | OtherNames= |Section1={{Chembox Identifiers | CASNo_Ref = | CASNo= 73145-13-8 | ChemSpiderID_Ref = | ChemSpiderID = 21864910 | PubChem=5460020 | ChEBI_Ref = | ChEBI = 28265 | SMILES= CC12CC(=O)NC13CC4C(C(C(=N4)CC5C(C6CCC(=O)C(=C7C(C(C(=CC(=N3)C2CCC(=O)O)[N-]7)CC(=O)O)CCC(=O)O)C6=N5)CC(=O)O)(C)CC(=O)N)CCC(=O)O.[Ni] | InChI = InChI=1S/C42H52N6O13.Ni/c1-40(16-30(43)50)22(5-9-33(54)55)27-15-42-41(2,17-31(51)48-42)23(6-10-34(56)57)26(47-42)13-24-20(11-35(58)59)19(4-8-32(52)53)39(45-24)37-28(49)7-3-18-21(12-36(60)61)25(46-38(18)37)14-29(40)44-27;/h13,18-23,25,27H,3-12,14-17H2,1-2H3,(H9,43,45,46,47,48,49,50,51,52,53,54,55,56,57,58,59,60,61);/p-1/t18-,19-,20-,21-,22+,23+,25+,27-,40-,41-,42-;/m0./s1 | InChIKey = QFGKGCZCUVIENT-SXMZNAGASA-M |Section2={{Chembox Properties | Formula= | MolarMass=906.58014 | Appearance=Yellow solid | Density= | MeltingPt= | BoilingPt= | Solubility= |Section3={{Chembox Hazards | MainHazards= | FlashPt= | AutoignitionPt = F430 is the cofactor (sometimes called the coenzyme) of the enzyme methyl coenzyme M reductase (MCR). MCR catalyzes the reaction that releases methane in the final step of methanogenesis: : ::data[format=table] | [[File:Coenzyme M (CoM).svg|class=skin-invert-image|left |thumb|Structure of coenzyme M (HS-CoM)]] | [[File:Coenzyme B (CoB).svg|class=skin-invert-image|thumb|Structure of coenzyme B (HS-CoB) |upright=1.5]] | |---|---| ::

It is found only in methanogenic Archaea and anaerobic methanotrophic Archaea. It occurs in relatively high concentrations in archaea that are involved in reverse methanogenesis; these can contain up to 7% by weight of the nickel protein.

Structure

The trivial name cofactor F430 was assigned in 1978 based on the properties of a yellow sample extracted from Methanobacterium thermoautotrophicum, which had a spectroscopic maximum at 430 nm. It was identified as the MCR cofactor in 1982 and the complete structure was deduced by X-ray crystallography and NMR spectroscopy. Coenzyme F430 features a reduced porphyrin in a macrocyclic ring system called a corphin. In addition, it possesses two additional rings in comparison to the standard tetrapyrrole (rings A-D), having a γ-lactam ring E and a keto-containing carbocyclic ring F. F430 and its biosynthetic precursors represent the only known biologically occurring tetrapyrroles containing nickel, an element rarely found in life.

Biosynthesis

::data[format=table] | [[File:Uroporphyrinogen III neutral.svg |left |thumb |uroporphyrinogen III]] | [[File:Precorrin-2.svg |thumb |dihydrosirohydrochlorin]] | [[File:Sirohydrochlorin.svg |thumb |sirohydrochlorin]] | |---|---|---| ::

The biosynthesis builds from uroporphyrinogen III, the progenitor of all natural tetrapyrroles, including chlorophyll, vitamin B12, phycobilins, siroheme, heme, and heme d1. It is converted to sirohydrochlorin via dihydrosirohydrochlorin. Insertion of nickel into this tetrapyrrole is catalysed in reaction by the same chelatase, CbiX, which inserts cobalt in the biosynthesis of cobalamin, here giving nickel(II)-sirohydrochlorin. ::figure[src="https://upload.wikimedia.org/wikipedia/commons/d/da/Biosynthesis_of_seco_Cofactor_F430.svg" caption="Nickel(II)-sirohydrochlorin a,c-diamide is converted to seco-F430. It is traditional to depict only one of four Ni-N bonds."] ::

The ATP-dependent Ni-sirohydrochlorin a,c-diamide synthase (CfbE) then converts the a and c acetate side chains to acetamide in reactions , generating nickel(II)-sirohydrochlorin a,c-diamide. The sequence of the two amidations is random. This enzyme is a MurF-like ligase, as found in peptidoglycan biosynthesis.

References

References

  1. (2014). "The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment". Springer.
  2. (2016). "Masters of methane". Nature Reviews Microbiology.
  3. Thauer RK. (1998). "Biochemistry of Methanogenesis: a Tribute to Marjory Stephenson". Microbiology.
  4. (December 2003). "A conspicuous nickel protein in microbial mats that oxidize methane anaerobically". Nature.
  5. (1978). "Chromophoric factors F342 and F430 of ''Methanobacterium'' thermoautotrophicum". FEMS Microbiology Letters.
  6. (1982). "Nickel-containing factor F430: Chromophore of the methylreductase of Methanobacterium". Proceedings of the National Academy of Sciences.
  7. (1991). "Coenzyme F430 from Methanogenic Bacteria : Complete Assignment of Configuration Based on an X-ray Analysis of 12,13-diepi-F430 Pentamethyl Ester and on NMR Spectroscopy". Helvetica Chimica Acta.
  8. (1986). "Chemistry of Corphinoids". Annals of the New York Academy of Sciences.
  9. (2 October 2017). "Metalloprotein Active Site Assembly". Wiley.
  10. (1985-10-07). "Sirohydrochlorin, a precursor of factor F430 biosynthesis in Methanobacterium thermoautotrophicum". FEBS Letters.
  11. (2017). "Elucidation of the biosynthesis of the methane catalyst coenzyme F430". Nature.
  12. (2016). "The biosynthetic pathway of coenzyme F430 in methanogenic and methanotrophic archaea". Science.
  13. R. Caspi. (2017-01-09). "Pathway: factor 430 biosynthesis". MetaCyc Metabolic Pathway Database.

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tetrapyrrolescofactorsnickel-compounds