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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Substrate free radicals are intermediates in ligninase catalysis.

The H2O2-requiring ligninase of the basidiomycete Phanerochaete chrysosporium oxidatively cleaves both lignin and lignin model compounds between C alpha and C beta ( C-1 and C-2) of their aliphatic side chains. Previous work has demonstrated a reaction mechanism by which ligninase oxidizes aromatic substrates to their cation radicals, which then undergo side chain cleavage to yield carbon-centered free radicals. These carbon-centered radicals add O2 to give substrate peroxyl radicals that react further to yield the hydroxylated and carbonylated end products usually seen in experiments with ligninase. To investigate this radical mechanism, we have now designed three dimeric lignin models: 1-(3,4-dimethoxyphenyl)-2-phenylethanol (I), 1-(3,4-dimethoxyphenyl)-2-phenylpropanol (II), and 1-(3,4-dimethoxyphenyl)-2-methyl-2-phenylpropanol (III). The following results were obtained when these models were oxidized by ligninase: methyl groups at C beta of the substrate favored C alpha-C beta cleavage versus C alpha oxidation to the ketone. GC/MS and HPLC analysis showed that II gave a radical coupling dimer, 2,3-diphenylbutane, as a major (26% yield) reaction product under anaerobic conditions. The anaerobic oxidation of III yielded 2,3-dimethyl-2,3-diphenylbutane. Spin-trapping experiments with nitrosobenzene showed that model II oxidation produced alpha-methylbenzyl radicals, whereas model III oxidation gave alpha, alpha-dimethylbenzyl radicals. TLC and iodometric determinations showed that III gave cumene hydroperoxide as a major (21% yield) reaction product in air. These findings demonstrate that carbon-centered and peroxyl radicals at C beta are major products of C alpha-C beta cleavage by ligninase.[1]


  1. Substrate free radicals are intermediates in ligninase catalysis. Hammel, K.E., Kalyanaraman, B., Kirk, T.K. Proc. Natl. Acad. Sci. U.S.A. (1986) [Pubmed]
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