My watch list
my.chemeurope.com  
Login  

Methyl-coenzyme M reductase



Methyl-coenzyme M reductase (MCR) is an enzyme that occurs in archaea and catalyzes the formation of methane by combining the hydrogen donor coenzyme B and the methyl donor coenzyme M. The enzyme has two active sites, each occupied by the nickel-containing F430 cofactor.[1] This conversion is symbolically written as:

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

References

  1. ^ Thauer, R. K., "Biochemistry of methanogenesis: a tribute to Marjory Stephenson", Microbiology, 1998, 144, 2377-2406. PMID 9782487

 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Methyl-coenzyme_M_reductase". A list of authors is available in Wikipedia.
Your browser is not current. Microsoft Internet Explorer 6.0 does not support some functions on Chemie.DE