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Literature summary extracted from

  • Ferapontova, E.E.; Castillo, J.; Gorton, L.
    Bioelectrocatalytic properties of lignin peroxidase from Phanerochaete chrysosporium in reactions with phenols, catechols and lignin-model compounds (2006), Biochim. Biophys. Acta, 1760, 1343-1354.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.11.1.14 analysis different mechanisms for the bioelectrocatalysis of the enzyme depend on the chemical nature of the mediators and are of a special interest both for fundamental science and for application of the enzyme as solid-phase bio(electro)catalyst for decomposition/detection of of recalcitrant aromatic compounds Phanerodontia chrysosporium

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.11.1.14 additional information
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 additional information bioelectric oxidation of organic substrates by LiP immobilized on graphite electrode Phanerodontia chrysosporium

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.14 Phanerodontia chrysosporium
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.14 additional information bioelectric oxidation of organic substrates by LiP immobilized on graphite electrodes: the enzyme can establish direct (i.e. mediatorless) electronic contact with graphite electrodes. In the case of the so called direct electron transfer reaction, the oxidized enzyme is directly reduced by the electrode to the initial ferriperoxidase state. In the presence of an electron donor other than electrode, the two-electron reduction of enzyme form E1 (containing an oxyferryl iron and a porphyrin pi cation radical) to the initial ferriperoxidase occurs through the intermediate formation of enzyme form II by a sequential one-electron transfer from the electron donor. The formed oxidized electron donor is then electrochemically reduced by the electrode. Different mechanisms for the bioelectrocatalysis of the enzyme depend on the chemical nature of the mediators and are of a special interest both for fundamental science and for application of the enzyme as solid-phase bio(electro)catalyst for decomposition/detection of of recalcitrant aromatic compounds Phanerodontia chrysosporium ?
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 ?
1.11.1.14 veratryl alcohol + H2O2
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 Phanerodontia chrysosporium 3,4-dimethoxybenzaldehyde + H2O
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 ?