Dream Peroxygenases

Dear Colleagues,

Functionally, peroxygenases (EC 1.11.2) are enzymes that catalyze the insertion of an oxygen atom from H₂O₂ into a variety of substrates. They include fungal (e.g., EC 1.11.2.1), animal (e.g., EC 1.11.2.2), plant (e.g., EC 1.11.2.3) and bacterial (such as EC 1.11.2.4 and other cytochrome P450s) enzymes using peroxide as the final electron acceptor and heme as a cofactor.

Among these, the fungal peroxygenases discovered by Prof Martin Hofrichter and coworkers (TU Dresden, Zittau, Germany), and also known as unspecific peroxygenases (UPOs), have emerged as "dream biocatalysts" of the greatest biotechnological interest because they catalyze the oxyfunctionalization of a wide substrate spectrum, often with exquisite regio- and stereo-selectivity. Among the reactions catalyzed by UPOs are the hydroxylation, epoxidation and dealkylation of aromatic and aliphatic compounds, oxidation of organic hetero-atoms and inorganic halides, as well as one-electron oxidation. The substrate diversity of fungal peroxygenases and the product patterns show similarities to P450s and enzymes classified as classical peroxidases, although the above protein families are phylogenetically unrelated.

This Special Issue will collect papers dealing with all aspects of peroxygenases, with a focus on those of the highest biotechnological interest, including genomic screening, heterologous expression, enzyme production, oxygenation reactions, enzyme engineering and process engineering. We aim to provide an updated overview of the state of the art in these enzymes, with papers describing recent developments in structural–functional relationships and optimized syntheses of fine chemicals and pharmaceuticals being especially welcome.

As Guest Editors, we invite you to contribute to the Special Issue on “Dream Peroxygenases”. Original research reports and reviews will be published online in Antioxidants.

Prof. Angel T. Martínez
Prof. Ana Gutiérrez
Guest Editors

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