Editing Methanogenesis (section)

===Proposed mechanism===
The biochemistry of methanogenesis involves the following coenzymes and cofactors: [[Coenzyme F420|F420]], [[coenzyme B]], [[coenzyme M]], [[methanofuran]], and [[methanopterin]].

The mechanism for the conversion of {{chem|CH|3|–S}} bond into methane involves a ternary complex of the enzyme, with the substituents forming a structure α<sub>2</sub>β<sub>2</sub>γ<sub>2</sub>. Within the complex, methyl coenzyme M and coenzyme B fit into a channel terminated by the axial site on nickel of the [[cofactor F430]].<ref>{{cite journal |last1=Cedervall |first1=Peder |title=Structural Insight into Methyl-Coenzyme M Reductase Chemistry Using Coenzyme B Analogues |journal=Biochemistry |date=22 July 2010 |volume=49 |issue=35 |pages=7683–7693 |doi=10.1021/bi100458d |pmid=20707311 |pmc=3098740 }}</ref>  One proposed mechanism invokes electron transfer from Ni(I) (to give Ni(II)), which initiates formation of {{chem|CH|4}}.  Coupling of the coenzyme M [[thiyl radical]] (RS<sup>.</sup>) with HS coenzyme B releases a proton and re-reduces Ni(II) by one electron, regenerating Ni(I).<ref>{{cite journal  |vauthors=Finazzo C, Harmer J, Bauer C, etal |title=Coenzyme B induced coordination of coenzyme M via its thiol group to Ni(I) of F<sub>430</sub> in active methyl-coenzyme M reductase |journal=J. Am. Chem. Soc. |volume=125 |issue=17 |pages=4988–9 |date=April 2003 |pmid=12708843 |doi=10.1021/ja0344314 |bibcode=2003JAChS.125.4988F }}</ref>