Tetrapyrroles pp 352-374 | Cite as

Role of Coenzyme F430 in Methanogenesis

  • Evert C. Duin
Part of the Molecular Biology Intelligence Unit book series (MBIU)


Methane production by methanogenic archaea takes place in many anaerobic microbial habitats such as swamps, rice paddies, fresh water sediments and the intestinal tract of animals and insects. Almost all species of methanogenic archaea are able to oxidize H2 and to use CO2 as the electron acceptor. Species from several families are also able to use formate, methanol, methylamine, and acetate. Although every pathway starts out different, they all end with the same step, the reduction of methyl-coenzyme M (CH3-S-CoM) with coenzyme B (HS-CoB) to CH4 and the mixed disulfide of coenzyme M and coenzyme B, CoM-S-S-CoB. This step is catalyzed by methyl-coenzyme M reductase (MCR). The enzyme contains a tightly bound nickel porphinoid, Factor 430 (F430). For the enzyme to be active the nickel has to be in the Ni(I) state. Although the enzyme was first isolated in 1981, only in recent years have we seen the development of methods to purify highly active MCR. This opened up the way to study the different states of MCR with spectroscopic methods including electron paramagnetic resonance, electron nuclear double resonance, resonance Raman, X-ray absorption, and magnetic circular dichroism spectroscopies. Here, I will present an overview of the most important findings and how these relate to the proposed reaction mechanisms as discussed in the literature.


Electron Paramagnetic Resonance Electron Paramagnetic Resonance Spectrum Electron Paramagnetic Resonance Signal Methanogenic Archaea Thiyl Radical 
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Copyright information

© Landes Bioscience and Springer Science+Business Media 2009

Authors and Affiliations

  1. 1.Department of Chemistry and BiochemistryAuburn UniversityAuburnUSA

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