1370087-83-4Relevant academic research and scientific papers
Model studies of methyl CoM reductase: Methane formation via CH 3-S bond cleavage of Ni(I) tetraazacyclic complexes having intramolecular methyl sulfide pendants
Nishigaki, Jun-Ichi,Matsumoto, Tsuyoshi,Tatsumi, Kazuyuki
, p. 5173 - 5187 (2012)
The Ni(I) tetraazacycles [Ni(dmmtc)]+ and [Ni(mtc)]+, which have methylthioethyl pendants, were synthesized as models of the reduced state of the active site of methyl coenzyme M reductase (MCR), and their structures and redox properties were elucidated (dmmtc, 1,8-dimethyl-4,11- bis{(2-methylthio)ethyl}-1,4,8,11-tetraaza-1,4,8,11-cyclotetradecane; mtc, 1,8-{bis(2-methylthio)ethyl}-1,4,8,11-tetraaza-1,4,8,11-cyclotetradecane). The intramolecular CH3-S bond of the thioether pendant of [Ni I(dmmtc)](OTf) was cleaved in THF at 75 °C in the presence of the bulky thiol DmpSH, which acts as a proton source, and methane was formed in 31% yield and a Ni(II) thiolate complex was concomitantly obtained (Dmp = 2,6-dimesityphenyl). The CH3-S bond cleavage of [Ni I(mtc)]+ also proceeded similarly, but under milder conditions probably due to the lower potential of the [NiI(mtc)] + complex. These results indicate that the robust CH3-S bond can be homolytically cleaved by the Ni(I) center when they are properly arranged, which highlights the significance of the F430 Ni environment in the active site of the MCR protein.
