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Title: Physiological importance of the heterodisulfide of coenzyme M and 7-mercaptoheptanoylthreonine phosphate in the reduction of carbon dioxide to methane in Methanobacterium

Journal Article · · Proc. Natl. Acad. Sci. U.S.A.; (United States)
DOI:https://doi.org/10.1073/pnas.85.1.60· OSTI ID:6470042

The heterodisulfide of the two coenzymes 2-mercaptoethanesulfonic acid (coenzyme M, HS-CoM) and N-(7-mercaptoheptanoyl)threonine O/sup 3/-phosphate (HS-HTP) increased the rate of CO/sub 2/ reduction to methane by cell extracts 42-fold. The stimulation resulted from activation of the initial step of methanogenesis, the production of formylmethanofuran from methanofuran and CO/sub 2/. These results establish a role for this heterodisulfide (CoM-S-S-HTP) in the reduction of CO/sub 2/ to formylmethanofuran. Evidence indicates that CoM-S-S-HTP is the labile intermediate that accounts for the coupling of the reduction of 2-(methylthio)ethanesulfonic acid by the methylreductase to formylmethanofuran biosynthesis, the RPG effect. The heterodisulfide was found to be labile in cell extracts due to enzyme-catalyzed reduction and possibly thiol-disulfide exchange.

Research Organization:
Univ. of Illinois, Urbana (USA)
DOE Contract Number:
FG02-87ER13651
OSTI ID:
6470042
Journal Information:
Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 85:1
Country of Publication:
United States
Language:
English