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Oxidation reactions catalyzed by manganese peroxidase isoenzymes from Ceriporiopsis subvermispora
Author(s) -
Urzúa Ulises,
Larrondo Luis Fernando,
Lobos Sergio,
Larraín Juan,
Vicuña Rafael
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00874-9
Subject(s) - chemistry , hydrogen peroxide , guaiacol , manganese peroxidase , oxalate , manganese , peroxidase , peroxide , nuclear chemistry , isoelectric point , catalysis , oxalic acid , biochemistry , inorganic chemistry , organic chemistry , enzyme
A total of 11 manganese peroxidase isoenzymes (MnP 1 ‐MnP 11 ) with isoelectric points (pIs) in the range of 4.58–3.20 were isolated from liquid‐ and solid‐state cultures of the basidiomycete Ceriporiopsis subvermispora . In the presence of hydrogen peroxide, these isoenzymes showed different requirements for Mn(II) in the oxidation of vanillylacetone, o ‐dianisidine, p ‐anisidine and ABTS, whereas oxidation of guaiacol by any isoenzyme did not take place when this metal was omitted. K m values for o ‐dianisidine and p ‐anisidine in the absence of Mn(II) are in the range of 0.5–1.0 mM and 4.5–42.0 mM, respectively. Oxalate and citrate, but not tartrate, accelerate the oxidation of o ‐dianisidine, both in the presence and in the absence of Mn(II). MnPs from this fungus are able to oxidize kojic acid without externally added hydrogen peroxide, indicating that they can also act as oxidases. In this reaction, however, the requirement for Mn(II) is absolute.