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- W2983223525 abstract "A mechanism has been previously proposed for methyl-coenzyme M (H/sub 3/CSCH/sub 2/CH/sub 2/SO/sub 3//sup /minus//) reductase where Ni/sup II/F/sub 430/ is first reduced to NiF/sub 430/, which homolytically cleaves the methyl-coenzyme M to produce methyl-Ni/sup I/F/sub 430/ followed by the protonation of methyl-Ni/sup I/F/sub 430/ to yield CH/sub 4/ and Ni/sup II/F/sub 430/. The role of the nickel ion oxidation state in methyl-coenzyme M catalysis has been examined. It was found that both the mono- and divalent oxidation states of the water soluble Ni (dioxo(16)-aneN/sub 5/), NiL, complex catalyze the methyl-coenzyme M to methane and coenzyme M. Some aqueous solutions of other nickel compounds, e.g. nickel (II) acetate, nickel(II) tetraethylenepentamine, or nickel(II) 1,4,8,11-tetraazacyclotetradecane-5,7-dione, do not convert methyl-coenzyme M to methane under argon or hydrogen. 30 references, 1 figure." @default.
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- W2983223525 date "1988-07-13" @default.
- W2983223525 modified "2023-09-28" @default.
- W2983223525 title "Ni/sup II/(dioxo(16)aneN/sub 5/)-induced methane formation from methyl coenzyme M" @default.
- W2983223525 hasPublicationYear "1988" @default.
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