Abstract
A cell-free system from a Pseudomonas sp., strain PM3, catalysed the oxidative demethylation, hydroxylation and subsequent ring cleavage of p-methoxybenzoate. Demethylation, to yield p-hydroxybenzoate, involved absorption of 1.0 mole of oxygen/mole of p-methoxybenzoate, and required reduced pyridine nucleotide (either NADH or NADPH) as cofactor. p-Hydroxybenzoate was hydroxylated to yield protocatechuate with the absorption of 1 mole of oxygen/mole of substrate, and required NADPH as cofactor. Protocatechuate was oxidized, with absorption of 1 mole of oxygen/mole of substrate, to 3-oxoadipate. The methyl group of p-methoxybenzoate was removed as formaldehyde, and oxidized to formate and carbon dioxide by formaldehyde dehydrogenase, which required GSH and NAD+, and formate dehydrogenase, which required NAD+.
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