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Cofactor F430 information


Cofactor F430
Identifiers
CAS Number
  • 73145-13-8 checkY
3D model (JSmol)
  • Interactive image
ChEBI
  • CHEBI:28265 checkY
ChemSpider
  • 21864910 checkY
PubChem CID
  • 5460020
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
    Key: QFGKGCZCUVIENT-SXMZNAGASA-M
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]
Properties
Chemical formula
C
42
H
51
N
6
NiO
13
Molar mass 906.58014
Appearance Yellow solid
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
Infobox references

F430 is the cofactor (sometimes called the coenzyme) of the enzyme methyl coenzyme M reductase (MCR).[1][2] MCR catalyzes the reaction EC 2.8.4.1 that releases methane in the final step of methanogenesis:

CH
3
–S–CoM
+ HS–CoB → CH
4
+ CoB–S–S–CoM
Structure of coenzyme M (HS-CoM)
Structure of coenzyme B (HS-CoB)

It is found only in methanogenic Archaea[3] 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.[4]

  1. ^ Stephen W., Ragdale (2014). "Biochemistry of Methyl-Coenzyme M Reductase: The Nickel Metalloenzyme that Catalyzes the Final Step in Synthesis and the First Step in Anaerobic Oxidation of the Greenhouse Gas Methane". In Peter M.H. Kroneck and Martha E. Sosa Torres (ed.). The Metal-Driven Biogeochemistry of Gaseous Compounds in the Environment. Metal Ions in Life Sciences. Vol. 14. Springer. pp. 125–145. doi:10.1007/978-94-017-9269-1_6. ISBN 978-94-017-9268-4. PMID 25416393.
  2. ^ Hofer, Ursula (2016). "Masters of methane". Nature Reviews Microbiology. 14 (12): 727. doi:10.1038/nrmicro.2016.170. PMID 27818502. S2CID 35175663.
  3. ^ Thauer RK (1998). "Biochemistry of Methanogenesis: a Tribute to Marjory Stephenson". Microbiology. 144 (9): 2377–2406. doi:10.1099/00221287-144-9-2377. PMID 9782487.
  4. ^ Krüger M, Meyerdierks A, Glöckner FO, et al. (December 2003). "A conspicuous nickel protein in microbial mats that oxidize methane anaerobically". Nature. 426 (6968): 878–81. Bibcode:2003Natur.426..878K. doi:10.1038/nature02207. PMID 14685246. S2CID 4383740.

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Cofactor F430

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F430 is the cofactor (sometimes called the coenzyme) of the enzyme methyl coenzyme M reductase (MCR). MCR catalyzes the reaction EC 2.8.4.1 that releases...

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F430

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F430 may refer to: Cofactor F430, F430, the prosthetic group of the enzyme methyl coenzyme M reductase Farman F.430, a 1930s French light transport aircraft...

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Porphyrin

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the highly reduced porphyrin coordinated to nickel that binds the Cofactor F430 active site in methyl coenzyme M reductase (MCR) Nitrogen-substituted...

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Nickel

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reduction of protons to form hydrogen gas. A nickel-tetrapyrrole coenzyme, cofactor F430, is present in methyl coenzyme M reductase, which can catalyze the formation...

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Prosthetic group

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property. Prosthetic groups are a subset of cofactors. Loosely bound metal ions and coenzymes are still cofactors, but are generally not called prosthetic...

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Heme

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heme. In bacteria, it also produces more complex substances such as cofactor F430 and cobalamin (vitamin B12). The pathway is initiated by the synthesis...

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Methanogenesis

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B fit into a channel terminated by the axial site on nickel of the cofactor F430. One proposed mechanism invokes electron transfer from Ni(I) (to give...

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Bioorganometallic chemistry

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final step, the scission of a nickel–methyl bond in cofactor F430. The iron–molybdenum cofactor (FeMoco) of nitrogenases contains an Fe6C unit and is...

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Chelatase

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sirohydrochlorin also requires a chelatase as part of the biosynthesis of cofactor F430. Apparently that chelatase is identical to the cobalt chelatase. Kaushik...

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Dihydrosirohydrochlorin

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enzymes. Further biosynthetic transformations convert sirohydrochlorin to cofactor F430 for an enzyme which catalyzes the release of methane in the final step...

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Sirohydrochlorin

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sulfite reductase enzymes. It is also the biosynthetic precursor to cofactor F430, an enzyme which catalyzes the release of methane in the final step...

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Bacteriochlorophyll

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uroporphyrinogen III in a separate pathway that leads, for example, to siroheme, cofactor F430 and cobalamin. The common intermediate is sirohydrochlorin. Niel, C...

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Coenzyme B

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catalyzed by the enzyme methyl coenzyme M reductase, which contains cofactor F430 as the prosthetic group. A related conversion that utilizes both HS-CoB...

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Abelsonite

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Alternative source are Methanogen Archea, where close compound is used in Cofactor F430 critical for methane production. In 2003, abelsonite was fully synthesized...

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Methanosarcina

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strains able to grow readily on acetate. A nickel-tetrapyrrole coenzyme, cofactor F430, is present in methyl coenzyme M reductase, which catalyzes the final...

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Sirohydrochlorin cobaltochelatase

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enzyme which inserts nickel into sirohydrochlorin in the biosynthesis of cofactor F430, reaction EC 4.99.1.11. Cobalamin biosynthesis As of late 2007, two...

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Nickel compounds

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bis(dimethylglyoximate), an insoluble red solid is important for gravimetric analysis. Cofactor F430 contains nickel in a tetrapyrrole derivative, and is used in the production...

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Coenzyme M

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catalyzed by the enzyme methyl-coenzyme M reductase, which restricts cofactor F430 as the prosthetic group. Coenzyme M is also used to make acetoacetate...

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Chlorophyllide

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latter is the first macrocyclic intermediate common to haem, sirohaem, cofactor F430, cobalamin and chlorophyll itself. The next intermediates are coproporphyrinogen...

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Methanogen

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and coenzyme F430. HS-HTP donates electrons to methyl-coenzyme M allowing the formation of methane and mixed disulfide of HS-CoM. F430, on the other...

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Ralph Stoner Wolfe

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Ellefson, W. L.; Whitman, W. B.; Wolfe, R. S. (1982). "Nickel-containing factor F430: Chromophore of the methylreductase of Methanobacterium". Proceedings of...

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Evolution of metal ions in biological systems

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biological systems. In proteins, it is found in a variety of sites and cofactors, including, for instance, haem groups, Fe–O–Fe sites, and iron–sulfur...

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