AbstractThe O2-dependent formation of side products during the oxidation of veratryl alcohol (VA) by lignin peroxidase has previously been proposed to start with the attack of H2O on the VA radical cation (VA+). This initial reaction is unlikely since it would also lead to side product formation in the absence of O2, which is not the case. In the current mechanism VA+ reacts first with O2, whereafter H2O attacks. Furthermore, this paper describes an alternative explanation for the inhibitory effect of Mn2+ on VA side product formation. It is proposed that Mn2+ reduces reactive intermediates back to VA
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to bri...
LiP (lignin peroxidase) from Trametopsis cervina has an exposed catalytic tyrosine residue (Tyr181) ...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...
The O2-dependent formation of side products during the oxidation of veratryl alcohol (VA) by lignin ...
AbstractThe O2-dependent formation of side products during the oxidation of veratryl alcohol (VA) by...
Lignin peroxidase (LiP), manganese-dependent peroxidase (MnP) and laccase are extracellular enzymes ...
AbstractThe oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium wa...
The kinetics of decay of veratryl alcohol radical cation, generated by cerium(IV) ammonium nitrate i...
The mechanism by which lignin peroxidase (Lip) interacts with the lignin polymer is discussed. Verat...
AbstractDegradation of 2-hydroxy-1,4-naphthoquinone (HNQ) by lignin peroxidase is discussed. Degrada...
Lignin peroxidase (LiP) and its natural substrate veratryl alcohol (VA) play a crucial role in ligni...
9 p.-3 fig.-4 tab.Lignin peroxidase (LiP) and its natural substrate veratryl alcohol (VA) play a cru...
The intramolecular kinetic deuterium isotope effects (k(H)/k(D) =4.6-4.9) determined in the H2O2-ind...
AbstractEnzymatic oxidation of veratryl alcohol yielded a new ring cleavage product (δ-lactone) in a...
A number of peroxidases, such as lignin peroxidase and manganese peroxidase have proved to be useful...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to bri...
LiP (lignin peroxidase) from Trametopsis cervina has an exposed catalytic tyrosine residue (Tyr181) ...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...
The O2-dependent formation of side products during the oxidation of veratryl alcohol (VA) by lignin ...
AbstractThe O2-dependent formation of side products during the oxidation of veratryl alcohol (VA) by...
Lignin peroxidase (LiP), manganese-dependent peroxidase (MnP) and laccase are extracellular enzymes ...
AbstractThe oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium wa...
The kinetics of decay of veratryl alcohol radical cation, generated by cerium(IV) ammonium nitrate i...
The mechanism by which lignin peroxidase (Lip) interacts with the lignin polymer is discussed. Verat...
AbstractDegradation of 2-hydroxy-1,4-naphthoquinone (HNQ) by lignin peroxidase is discussed. Degrada...
Lignin peroxidase (LiP) and its natural substrate veratryl alcohol (VA) play a crucial role in ligni...
9 p.-3 fig.-4 tab.Lignin peroxidase (LiP) and its natural substrate veratryl alcohol (VA) play a cru...
The intramolecular kinetic deuterium isotope effects (k(H)/k(D) =4.6-4.9) determined in the H2O2-ind...
AbstractEnzymatic oxidation of veratryl alcohol yielded a new ring cleavage product (δ-lactone) in a...
A number of peroxidases, such as lignin peroxidase and manganese peroxidase have proved to be useful...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to bri...
LiP (lignin peroxidase) from Trametopsis cervina has an exposed catalytic tyrosine residue (Tyr181) ...
A manganese-peroxidase from Lentinus edodes solid-state cultures was purified and its ability to...