Coenzyme-B sulfoethylthiotransferase

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Coenzyme-B sulfoethylthiotransferase

In enzymology, coenzyme-B sulfoethylthiotransferase, also known as methyl-coenzyme M reductase (MCR) or most systematically as 2-(methylthio)ethanesulfonate:N-(7-thioheptanoyl)-3-O-phosphothreonine S-(2-sulfoethyl)thiotransferase is an enzyme that catalyzes the final step in the formation of methane.[1] It does so by combining the hydrogen donor coenzyme B and the methyl donor coenzyme M. Via this enzyme, most of the natural gas on earth was produced. Ruminants (e.g. cows) produce methane because their rumens contain methanogenic prokaryotes (Archaea)[2][3] that encode and express the set of genes of this enzymatic complex.

The enzyme has two active sites, each occupied by the nickel-containing F430 cofactor.[4]

methyl-CoM2-(methylthio)ethanesulfonate + coenzyme BN-(7-mercaptoheptanoyl)threonine 3-O-phosphate CoM-S-S-CoB + methane
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Structure of 2-mercaptoethanesulfonate (coenzyme M: reacts after methylation on the thiol)
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Structure of N-(7-mercaptoheptanoyl)threonine 3-O-phosphate (coenzyme B)

The two substrates of this enzyme are 2-(methylthio)ethanesulfonate and N-(7-mercaptoheptanoyl)threonine 3-O-phosphate; its two products are CoM-S-S-CoB and methane. 3-Nitrooxypropanol inhibits the enzyme.[5]

In some species, the enzyme reacts in reverse (a process called reverse methanogenesis), catalysing the anaerobic oxidation of methane, therefore removing it from the environment.[6] Such organisms are methanotrophs.

This enzyme belongs to the family of transferases, specifically those transferring alkylthio groups.

Structure

Coenzyme-B sulfoethylthiotransferase is a multiprotein complex made up of a pair of identical halves. Each half is made up of three subunits: α, β and γ,[7] also called McrA, McrB and McrG, respectively.

References

Further reading

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