Michael A Schätzle

Publications (3)29.22 Total impact

• Article: Tautomers of anthrahydroquinones: enzymatic reduction and implications for chrysophanol, monodictyphenone, and related xanthone biosyntheses.

  Michael A Schätzle, Syed Masood Husain, Sascha Ferlaino, Michael Müller
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  ABSTRACT: Reduction of emodin by sodium dithionite resulted in the formation of two tautomeric forms of emodin hydroquinone. Subsequent conversion by the short-chain dehydrogenase/reductase (SDR) MdpC into the corresponding 3-hydroxy-3,4-dihydroanthracen-1(2H)-one implies that deoxygenation is the first step in monodictyphenone biosynthesis. Implications for chrysophanol formation as well as reaction sequences in the related xanthone, ergochrome, and bianthraquinone biosyntheses are discussed.
  Journal of the American Chemical Society 08/2012; 134(36):14742-5. · 9.91 Impact Factor
• Article: Biomimetic Asymmetric Synthesis of (R)-GTRI-02 and (3S,4R)-3,4-Dihydroxy-3,4-dihydronaphthalen-1(2H)-ones.

  Syed Masood Husain, Michael A Schätzle, Caroline Röhr, Steffen Lüdeke, Michael Müller
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  ABSTRACT: The NADPH-dependent tetrahydroxynaphthalene reductase (T(4)HNR) from Magnaporthe grisea was used for the biomimetic synthesis of (R)-GTRI-02 by stereoselective reduction of 1-(3,6,8-trihydroxy-1-methylnaphthalen-2-yl)ethanone. This also led to the isolation of a (3S,4R)-cis-ketodiol formed by T(4)HNR-catalyzed reduction of the corresponding hydroxynaphthoquinone. Flaviolin and lawsone also reduced to corresponding cis-ketodiols in good yields.
  Organic Letters 06/2012; · 5.86 Impact Factor
• Article: Tetrahydroxynaphthalene reductase: catalytic properties of an enzyme involved in reductive asymmetric naphthol dearomatization.

  Michael A Schätzle, Stephan Flemming, Syed Masood Husain, Michael Richter, Stefan Günther, Michael Müller
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  ABSTRACT: In reduced circumstances: tetrahydroxynaphthalene reductase shows a broad substrate range including alternate phenolic compounds and cyclic ketones. Structural modeling reveals major enzyme-substrate interactions; C-terminal truncation of the enzyme causes an altered substrate preference, in accordance with stabilization of the substrate by the C-terminal carboxylate. This effect allows the identification of a homologous enzyme.
  Angewandte Chemie International Edition 02/2012; 51(11):2643-6. · 13.45 Impact Factor