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CAS number
PubChem 5460020
Molecular formula C42H51N6NiO13-
Molar mass 906.58014
Except where noted otherwise, data are given for
materials in their standard state
(at 25 °C, 100 kPa)

Infobox disclaimer and references

F430 is the prosthetic group of the enzyme methyl coenzyme M reductase. It is found only in methanogenic archaea.[1] This enzyme catalyzes the release of methane in the final step of methanogenesis:

CH3-S-CoM + HS-CoB → CH4 + CoB-S-S-CoM


Corphin in context

Nature uses many tetrapyrroles - hemes, chlorophyll, and vitamin B12. F430 is the most reduced tetrapyrrole in nature with only five double bonds. This particular tetrapyrrole derivative is called a corphin. Because of its relative lack of conjugated unsaturation, it is yellow, not the intense purple-red associated with more unsaturated tetrapyrroles. It is also the only tetrapyrrole derivative found in nature to contain nickel. Ni(II) is too small for the N4 binding site of the corphin, which causes the macrocycle to adopt a ruffled structure.

Proposed mechanism of methanogenesis

The active form of F430 contains Ni(I), analogously to the reduced B12 cofactors that feature Co(I). Whereas Co(I) is d8 and diamagnetic, Ni(I) is d9 and paramagnetic. The mechanism by which Nature cleaves the CH3-S bond in methyl coenzyme M is presently (2006) unclear although it is known that both coenzyme M and coenzyme B fits into a channel terminated by the axial site on nickel. A plausible mechanism entails electron transfer from Ni(I) (to give Ni(II)), and this electron transfer initiates formation of CH4. Coupling of the coenzyme M thiyl radical with HS coenzyme B releases a proton and re-reduces Ni(II) by one-electron, regenerating Ni(I).[2]

Its structure was deduced by X-ray crystallography and NMR spectroscopy.[3]

Anaerobic methane oxidation

F430 occurs in very high concentrations in bacteria that are thought to be involved in reverse methanogenesis, where methane is converted to methyl coenzyme M. Organisms that promote this remarkable reaction contain 7% by weight nickel protein.[4]


  1. ^ Thauer, R. K., "Biochemistry of Methanogenesis: a Tribute to Marjory Stephenson", Microbiology, 1998, 144, 2377-2406
  2. ^ Finazzo, C.; Harmer, J.; Bauer, C.; Jaun, B.; Duin, E. C.; Mahlert, F.; Goenrich, M.; Thauer, R. K.; Van Doorslaer, S. and Schweiger, A., "Coenzyme B Induced Coordination of Coenzyme M via Its Thiol Group to Ni(I) of F430 in Active Methyl-Coenzyme M Reductase", Journal of the American Chemical Society, 2003, volume 125, 4988-4989.
  3. ^ Farber, G.; Keller, W.; Kratky, C.; Jaun, B.; Pfaltz, A.; Spinner, C.; Kobelt, A.; Eschenmoser, A. “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 1991, volume 74, pages 697-716.
  4. ^ Krüger, M.; Meyerdierks, A.; Glöckner, F. O.; Amann, R.; Widdel, F.; Kube, M.; Reinhardt, R.; Kahnt, J.; Böcher, R.; Thauer, R. K.; Shima, S., "A Conspicuous Nickel Protein in Microbial Mats that Oxidize Methane Anaerobically", Nature, 2003, volume 426, 878-881
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "F430". A list of authors is available in Wikipedia.
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