Enzymatic Production of Both Enantiomers of Rhododendrol

Musa M. Musa

Department of Chemistry, King Fahd University of Petroleum and Minerals, Dhahran 31261, Kingdom of Saudi Arabia

Corresponding author: Fax: +966 138604277; Tel: +966 138607343; E-mail: musam@kfupm.edu.sa


An asymmetric synthetic approach to produce (R)- and (S)-rhododendrol is described. W110A Thermoanaerobacter ethanolicus secondary alcohol dehydrogenase (W110A TeSADH), an (S)-specific mutant of TeSADH, is used in this approach. The enantioselective reduction of 4-(4'-hydroxyphenyl)-2-butanone catalyzed by W110A TeSADH yielded (S)-rhododendrol, the Prelog product. The anti-Prelog product, (R)-rhododendrol, is produced from (rac)-rhododendrol through enantiospecific kinetic resolution catalyzed by W110A TeSADH.


Alcohol dehydrogenases, Asymmetric reduction, Biotransformations, Kinetic resolution, Redox reactions, Rhododendrol.

Reference (17)

1.      K. Archangelsky, Arch. Exp. Path. Pharm, 46, 313 (1901); doi:10.1007/BF01977728.

2.      W.H. Tallent, J. Org. Chem., 29, 988 (1964); doi:10.1021/jo01027a539.

3.      M.H. Kim, A. Nugroho, J. Choi, J.H. Park and H.J. Park, Arch. Pharm. Res., 34, 971 (2011); doi:10.1007/s12272-011-0614-1.

4.      (a) G. Sabitha, B. Thirupathaiah and J. Yadav, Synth. Commun., 37, 1683 (2007); doi:10.1080/00397910701265614.; (b) Y. Yuasa, S. Shibuya and Y. Yuasa, Synth. Commun., 33, 1469 (2003); doi:10.1081/SCC-120018756.; (c) B. Das, S. Padma Rao, K.V.N.S. Srinivas and J.S. Yadav, Phytochemistry, 33, 1529 (1993); doi:10.1016/0031-9422(93)85127-D.; (d) T. Kitayama, S. Isomori and K. Nakamura, Tetrahedron Asymmetry, 24, 621 (2013); doi:10.1016/j.tetasy.2013.04.013.

5.      U.T. Bornscheuer, G.W. Huisman, R.J. Kazlauskas, S. Lutz, J.C. Moore and K. Robins, Nature, 485, 185 (2012); doi:10.1038/nature11117.

6.      F. Hollmann, I.W.C.E. Arends and D. Holtmann, Green Chem., 13, 2285 (2011); doi:10.1039/c1gc15424a.

7.      M. Hall and A.S. Bommarius, Chem. Rev., 111, 4088 (2011); doi:10.1021/cr200013n.

8.      D.S. Burdette and J.G. Zeikus, Biochem. J., 302, 163 (1994).

9.      D.S. Burdette, V.V. Tchernajencko and J.G. Zeikus, Enzyme Microb. Technol., 27, 11 (2000); doi:10.1016/S0141-0229(00)00192-7.

10.  M.M. Musa, K.I. Ziegelmann-Fjeld, C. Vieille and R.S. Phillips, Org. Biomol. Chem., 6, 887 (2008); doi:10.1039/b717120j.

11.  K.I. Ziegelmann-Fjeld, M.M. Musa, R.S. Phillips, J.G. Zeikus and C. Vieille, Protein Eng. Des. Sel., 20, 47 (2007); doi:10.1093/protein/gzl052.

12.  V. Prelog, Pure Appl. Chem., 9, 119 (1964); doi:10.1351/pac196409010119.

13.  M.M. Musa, R.S. Phillips, M. Laivenieks, C. Vieille, M. Takahashi and S.M. Hamdan, Org. Biomol. Chem., 11, 2911 (2013); doi:10.1039/c3ob27415b.

14.  A. Ghanem and V. Schurig, Tetrahedron Asymmetry, 14, 57 (2003); doi:10.1016/S0957-4166(02)00745-0.

15.  W. Kroutil, H. Mang, K. Edegger and K. Faber, Curr. Opin. Chem. Biol., 8, 120 (2004); doi:10.1016/j.cbpa.2004.02.005.

16.  M.M. Musa and R.S. Phillips, Catal. Sci. Technol., 1, 1311 (2011); doi:10.1039/c1cy00160d.

17.  M.M. Musa, K.I. Ziegelmann-Fjeld, C. Vieille, J.G. Zeikus and R.S. Phillips, J. Org. Chem., 72, 30 (2007); doi:10.1021/jo0616097.

   View Article PDF File Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.