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. Copyright © 1971, Wiley Blackwell. All rights reserved
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CITATION STYLE
Brändén, R., Malmström, B. G., & Vänngård, T. (1971). The Interaction of Fungal Laccase with Hydrogen Peroxide and the Removal of Fluoride from the Inhibited Enzyme. European Journal of Biochemistry, 18(2), 238–241. https://doi.org/10.1111/j.1432-1033.1971.tb01236.x
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