Max-Planck researchers unravel the structure of the methane forming enzyme
A team of the Max-Planck Institutes from Frankfurt and Marburg has recently determined the structure of methyl-coenzyme M reductase, a key enzyme of methanogenesis that catalyzes a highly complex chemical reaction namely the reduction of a thioether to a hydrocarbon.
Methanogenesis is only carried out by a group of strictly anaerobic microbes called methanogens which use the formation of methane for the purpose of cellular energy generation. Within the microbial ecosystem methanogens participate in the final step of anoxic decomposition of complex organic materials thereby producing about 109 tons of methane per year. The generated methane is either remetabolized by methanotrophic bacteria or escapes to the atmosphere as a potent greenhouse gas. All methanogens are dependent on the enzyme methyl-CoM reductase, a protein complex of 300 kDa size. Its crystal structure was solved to a resolution of 1.45 E which represents the highest resolution for biological macromolecules of that size so far.
Nature has evolved with methyl-coenzyme M reductase a remarkable enzyme composed of six subunits forming a heterohexamer in an (a,_,c)2 arrangement. Three unusual coenzymes are embedded in a 30 E long channel between the subunits. Of particular interest is the binding of coenzyme F430, a Ni-porphinoid which exclusively occurs in this enzyme. As substrates the enzyme binds methyl-coenzyme M (methyl-thioethane sulfonate) and coenzyme B (7-thioheptanoyl threoninephosphate). The highly resolved crystal structure allows a description of the binding modes of these 3exotic2 coenzymes within the protein on an atomic ground.
The biochemical reaction of methyl-coenzyme M reductase
proceeds by reducing of methyl-coenzyme M to methane and by
Contact: Ulrich Ermler