Reduction of H2O2-oxidized manganese peroxidase (MnP), lignin peroxida
se and, to some extent, horseradish peroxidase, was studied in the pre
sence of cellobiose oxidase (CbO) and cellobiose. It was found that th
e reversion rates for MnP compound II and lignin peroxidase compound I
I back to native enzymes increased significantly in the presence of Cb
O and cellobiose. However, the reduction of cytochrome c by CbO plus c
ellobiose was 40 times faster than the reduction of MnP compound II. A
lso, the lag phase before reversion to the native states decreased for
all three peroxidases in the presence of CbO and cellobiose. Active C
bO did not repress formation of compounds I or II of the peroxidases,
and Mn2+/veratryl alcohol reduced compound II of the peroxidases much
more rapidly than did active CbO. This indicates that, in the presence
of Mn2+ or veratryl alcohol, MnP and lignin peroxidase can complete t
heir catalytic cycles and function normally without interference from
CbO. Without the presence of peroxidase substrates, active CbO reduced
compound II of the above peroxidases.