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Am. Chem. Soc."},{"key":"10.1016\/j.abb.2020.108732_bib72","unstructured":"Britta Frensch, Thorsten Lechtenberg, Michel Kather, Zeynep Yunt, Martin Betschart, Bernd Kammerer, Steffen L\u00fcdeke, Michael M\u00fcller, J\u00f6rn Piel, Robin Teufel, Enzymatic Spiroketal Formation via Oxidative Rearrangement of Pentangular Polyketides (in revision)."},{"key":"10.1016\/j.abb.2020.108732_bib73","doi-asserted-by":"crossref","first-page":"22459","DOI":"10.1016\/S0021-9258(17)31664-2","article-title":"Activation of molecular oxygen by flavins and flavoproteins","volume":"269","author":"Massey","year":"1994","journal-title":"J. Biol. 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