1995
DOI: 10.1021/bi00039a018
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Abstract: It has recently been discovered that lignin peroxidase isozyme H2 (LiPH2) has the ability to oxidize Mn2+ (Khindaria et al., 1995). Furthermore, at pH 4.5, the physiological pH of Phanerochaete chrysosporium, LiPH2 oxidizes Mn2+ at a much faster rate (25 times) than veratryl alcohol (VA). The ability of Mn2+ to act as a redox mediator for indirect oxidations catalyzed by LiPH2 was therefore investigated. In the presence of physiologically relevant levels of oxalate and Mn2+, the rate of LiPH2-catalyzed oxidati… Show more

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Cited by 12 publications
(5 citation statements)
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“…Thus, LiP lacks an available, stable Mn II binding site. Although it recently has been claimed that one of the LiP isozymes, H2, can oxidize Mn II (Khindaria et al, 1995;Sutherland et al, 1995), comparison of the LiP-H2 sequence with those of MnP1 and LiP-H8 reveals that LiP-H2 also lacks a favorable Mn II binding site, and thus is unlikely to complete its catalytic cycle in the presence of Mn II as the only reducing substrate. Contamination of LiP-H2 with MnP during purification may account for the reported oxidation of Mn II (Khindaria et al, 1995;Sutherland et al, 1995).…”
Section: Discussionmentioning
confidence: 99%
“…Thus, LiP lacks an available, stable Mn II binding site. Although it recently has been claimed that one of the LiP isozymes, H2, can oxidize Mn II (Khindaria et al, 1995;Sutherland et al, 1995), comparison of the LiP-H2 sequence with those of MnP1 and LiP-H8 reveals that LiP-H2 also lacks a favorable Mn II binding site, and thus is unlikely to complete its catalytic cycle in the presence of Mn II as the only reducing substrate. Contamination of LiP-H2 with MnP during purification may account for the reported oxidation of Mn II (Khindaria et al, 1995;Sutherland et al, 1995).…”
Section: Discussionmentioning
confidence: 99%
“…Next, 100 mL of diluted enzyme was then added to 900 µL of assay buffer containing 1 mM H2O2, 1 mM CPZ, and 1 mM guaiacol. The reaction rate was determined by monitoring the increase in absorbance at 465 nm using an extinction coefficient of 6100 M -1 cm -1 for oxidized guaiacol (25). Percent remaining activity was determined by comparison with an identical enzyme aliquot taken at time zero.…”
Section: Methodsmentioning
confidence: 99%
“…OA excreted by wood degrading fungi (Shimada et al 1994;Dutton and Evans 1996) is thought to lead to hemicellulose degradation and cellulose depolymerisation (Green et al 1991). Oxidative reactions by manganese peroxidase which is produced by white rot fungi are enhanced by chelation of manganese ions by oxalate, providing greater solubility and oxidative action at a distance from the enzyme (Wariishi et al 1992;Kuan and Tien 1993;Kishi et al 1994;Sutherland et al 1995;Timofeevski and Aust 1997;Zapanta and Tien 1997). Oxidative actions involving oxalate can produce free radicals (Khindaria et al 1994), which might result in oxalate attachment.…”
Section: Changes In Wood Properties Due To Biopulpingmentioning
confidence: 99%