Anaerobic O-demethylations of methoxynaphthols, methoxyfuran, and fluoroanisols by Sporomusa ovata.

In vitro experiments with 3,4-dimethoxybenzoate-induced Sporomusa enzymes a broad O-methyl ether cleavage capacity. The O-demethylase activity hydrolized the methyl-oxygen linkages of methoxynaphtholes of the heterocycles 2-methoxyfuran or 2-methoxythiophene as well as of several dimethoxy and monomethoxy aryls under anaerobic conditions. Also, fluoro and chloro substituents of anisoles enhanced the O-demethylation rate, indicating that an electron delocalized aromatic structure supported the methyl ether activation mechanism.

Corrinoid-Dependent Methyl Transfer Reactions Are Involved in Methanol and 3,4-Dimethoxybenzoate Metabolism by Sporomusa ovata.

Washed and air-oxidized proteins from Sporomusa ovata cleaved the C-O bond of methanol or methoxyaromatics and transferred the methyl to dl-tetrahydrofolate. The reactions strictly required a reductive activation by titanium citrate, catalytic amounts of ATP, and the addition of dl-tetrahydrofolate. Methylcorrinoid-containing proteins carried the methanol methyl, which was transferred to dl-tetrahydrofolate at a specific rate of 120 nmol h mg of protein.