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A Simplified Assay for Coenzyme M (HSCH₂CH₂SO₃)

RESOLUTION OF METHYLCOBALAMIN-COENZYME M METHYLTRANSFERASE AND USE OF SODIUM BOROHYDRIDE

From the ¹ From the Department of Microbiology, University of Illinois, Urbana, Illinois 61801

The methylation of 2,2'-dithiodiethanesulfonic acid ((S-CoM)₂) by methylcobalamin-coenzyme M methyltransferase requires an additional acidic protein, when NADPH is used as the electron source. This protein component and NADPH may be replaced by sodium borohydride which acts by reducing (S-CoM)₂ to 2-mercaptoethanesulfonic acid (HS-CoM) prior to methylation. Evidence suggests that reduction by borohydride is chemical rather than enzyme directed. Catalysis by 100-fold purified methyltransferase requires only methylcobalamin and HS-CoM. The assay is accurate, reliable, and may be used to determine the usual enzyme kinetic parameters.

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