The Interaction of Fungal Laccase with Hydrogen Peroxide and the Removal of Fluoride from the Inhibited Enzyme
Authors:
- Rolf BrändénRBRolf Brändén
- B G MalmströmBMB G Malmström
- Bo G.BGBo G.
- Tore VänngårdTVTore Vänngård
- 1 January 1971
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 18 (2) , 238-241
Abstract
Electron paramagnetic resonance analysis shows that H2O2 added to native fungal laccase binds to one specific Cu2+ of the four copper atoms in the enzyme (the so‐called Type 2 or “nonblue” Cu2+). This binding of H2O2 is associated with a new absorption band in the visible and nearultraviolet spectrum of the enzyme with its maximum absorbance at 400 nm. Fluoride bound to Type 2 Cu2+ of the enzyme, as commonly prepared, can easily be removed by dialysis of the reduced enzyme. Presence of H2O2 in this dialysis makes the removal of fluoride faster.Keywords
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