When the crystal structure of P. chrysosporium LiP was
reported, it was assumed that this peroxidase would
oxidize high-redox-potential aromatic compounds at the
main haem access channel. In fact, veratryl alcohol was
modelled at the crystal structure channel to determine the
eventual contacts (Poulos et al., 1993). This is the classical
peroxidase substrate oxidation site, as shown in plant
HRP and in the low-redox-potential fungal CIP (Smith and
Veitch, 1998). However, the main haem access channel of
LiP is significantly narrower than those of CIP or HRP, and
the hypothesis of long-range electron transfer (LRET) oxidation
of lignin at the protein surface, initially proposed by
Du and colleagues (1992) and Schoemaker and colleagues
(1994), was adopted by other authors.
When the crystal structure of P. chrysosporium LiP wasreported, it was assumed that this peroxidase wouldoxidize high-redox-potential aromatic compounds at themain haem access channel. In fact, veratryl alcohol wasmodelled at the crystal structure channel to determine theeventual contacts (Poulos et al., 1993). This is the classicalperoxidase substrate oxidation site, as shown in plantHRP and in the low-redox-potential fungal CIP (Smith andVeitch, 1998). However, the main haem access channel ofLiP is significantly narrower than those of CIP or HRP, andthe hypothesis of long-range electron transfer (LRET) oxidationof lignin at the protein surface, initially proposed byDu and colleagues (1992) and Schoemaker and colleagues(1994), was adopted by other authors.
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