Acknowledgements
18 H. Korbekandi, P. Mather, J. Gardiner and G. Stephens, Enzyme
Microb. Technol., 2008, 42, 308–314.
This project was performed within the DK ‘Molecular Enzy-
mology’ and financial support by the Austrian Science Fund
FWF (Vienna, project W9) is gratefully acknowledged. Cordial
thanks go to R. Breinbauer (Graz) for his valuable comments
and to N. C. Bruce and H. Housden (University of York) for
their generous donation of N-ethylmaleimide-, morphinone-
and PETN-reductase.
19 N. J. Mueller, C. Stueckler, M. Hall, P. Macheroux and K. Faber,
Org. Biomol. Chem., 2009, 7, 1115–1119.
2
0 M. Hall, C. Stueckler, W. Kroutil, P. Macheroux and K. Faber,
Angew. Chem., Int. Ed., 2007, 46, 3934–3937.
21 M. Hall, C. Stueckler, H. Ehammer, E. Pointner, G. Oberdorfer, K.
Gruber, B. Hauer, R. Stuermer, P. Macheroux, W. Kroutil and K.
Faber, Adv. Synth. Catal., 2008, 350, 411–418.
2
2
2
2 A. M u¨ ller, B. Hauer and B. Rosche, Biotechnol. Bioeng., 2007, 98,
2–29.
3 M. Hall, C. Stueckler, B. Hauer, R. Stuermer, T. Friedrich, M. Breuer,
W. Kroutil and K. Faber, Eur. J. Org. Chem., 2008, 1511–1516.
4 (a) J. R. Snape, N. A. Walkley, A. P. Morby, S. Nicklin and G. F.
White, J. Bacteriol., 1997, 179, 7796–7802; (b) G. F. White, J. R.
Snape and S. Nicklin, Appl. Environ. Microbiol., 1996, 62, 637–642.
2
References
1
(a) J. C. Spain, Annu. Rev. Microbiol., 1995, 49, 523–555; (b) F. D.
Marvin-Sikkema and J. A. M. de Bont, Appl. Microbiol. Biotechnol.,
25 (a) J. J. Griese, R. P. Jakob, S. Schwarzinger and H. Dobbek, J. Mol.
Biol., 2006, 361, 140–152; (b) J. F. Chaparro-Riggers, T. A. Rogers, E.
Vazquez-Figueroa, K. M. Polizzi and A. S. Bommarius, Adv. Synth.
Catal., 2007, 349, 1521–1531.
26 The stereoselectivity of this transformation using PETN reductase
may vary to some extent and, depending on the reaction conditions,
even may switch to (S); H. S. Toogood, A. Fryszkowska, V. Hare,
K. Fisher, A. Roujeinikova, D. Leys, J. M. Gardiner, G. M. Stephens
and N. S. Scrutton, Adv. Synth. Catal., 2008, 350, 2798–2803.
27 (a) D. H. Aur and D. Thomas, J. Org. Chem., 1974, 39, 3855–3862;
(b) M. Witanowski, L. Stefaniak, H. Januszewski, S. Szymanski and
G. A. Webb, Tetrahedron, 1973, 29, 2833–2836.
28 (a) M. H. Millen and W. A. Waters, J. Chem. Soc. B, 1971, 2398–
2400; (b) J. S. B. Park and J. C. Walton, J. Chem. Soc., Perkin Trans.
2, 1997, 2579–2583; (c) R. Glaser, R. K. Murmann and C. L. Barnes,
J. Org. Chem., 1996, 61, 1047–1058; (d) A. Srinivasan, N. Kebede,
J. E. Saavedra, A. V. Nikolaitchik, D. A. Brady, E. Yourd, K. M.
Davies, L. K. Keefer and J. P. Toscano, J. Am. Chem. Soc., 2001,
123, 5465–5472; (e) N. W. Cant and I. O. Y. Liu, Catal. Today,
2000, 63, 133–146; (f) Y. L. Chow, J. N. S. Tam and K. S. Pillay,
Can. J. Chem., 1973, 51, 2477–2485; (g) J. Suwinski, K. Swierczek, P.
Wagner, M. Kubicki, T. Borowiak and J. Slowikowska, J. Heterocycl.
Chem., 2003, 40, 523–528.
1
994, 42, 499–507.
2
3
Z. C. Symons and N. C. Bruce, Nat. Prod. Rep., 2006, 23, 845–850.
J. L. Ramos, M. Mar Gonzalez-Perez, A. Caballero and P. van
Dillewijn, Curr. Opin. Biotechnol., 2005, 16, 275–281.
(a) C. L. Davey, L. W. Powell, N. J. Turner and A. Wells, Tetrahedron
Lett., 1994, 35, 7867–7870; (b) J. A. Blackie, N. J. Turner and A. S.
Wells, Tetrahedron Lett., 1997, 38, 3043–3046; (c) A. Navarro-Ocana,
L. F. Olguin, H. Luna, M. Jimenez-Estrada and E. Barzana, J. Chem.
Soc., Perkin Trans. 1, 2001, 2754–2756.
4
5
6
7
R. E. Williams, D. A. Rathbone, N. S. Scrutton and N. C. Bruce,
Appl. Environ. Microbiol., 2004, 70, 3566–3574.
W. W. Westerfeld, D. A. Richert and E. S. Higgins, J. Biol. Chem.,
1
957, 227, 379–391.
(a) S. Trivic, V. Leskovac, D. Pericin and G. W. Winston, Biotechnol.
Lett., 2002, 24, 807–812; (b) The reductive hydrolytic degradation of
oximes catalysed by nicotinamide-dependent alcohol dehydrogenases
was recently reported:B. Ferreira-Silva, I. Lavandera, A. Kern, K.
Faber and W. Kroutil, manuscript submitted.
8
9
(a) C. Bryant and M. Deluca, J. Biol. Chem., 1991, 266, 4119–4125;
(
b) C. Bryant, L. Hubbart and M. Deluca, FASEB J., 1988, 2, A1778–
A1778.
(a) V. Holler, D. Wegricht, I. Yuranov, L. Kiwi-Minsker and A.
Renken, Chem. Eng. Technol., 2000, 23, 251–255; (b) R.-M. Wittich,
A. Haidour, P. van Dillewijn and J.-L. Ramos, Environ. Sci. Technol.,
29 The rate of spontaneous hydrolysis of all oximes from this study was
below the limit of detectability (≤3%) under the reaction conditions
employed.
30 Based on stability tests, the hypothesis of the spontaneous hydrolysis
of the oxime can be ruled and, in addition, the occurrence of a
highly unstable N-hydroxy-enamine-species as intermediate is rather
unlikely.
2
008, 42, 734–739.
1
0 (a) C. E. French, S. J. Rosser, G. J. Davies, S. Nicklin and N. C. Bruce,
Nat. Biotechnol., 1999, 17, 491–494; (b) J. W. Pak, K. L. Knoke, D. R.
Noguera, B. G. Fox and G. H. Chambliss, Appl. Environ. Microbiol.,
2
000, 66, 4742–4750; (c) M. M. Gonzalez-Perez, P. van Dillewijn,
R. M. Wittich and J. L. Ramos, Environ. Microbiol., 2007, 9, 1535–
540.
31 Although the Nef-reaction was originally invented as the (redox-
neutral) hydrolysis of prim- and sec-nitroalkanes to yield the cor-
1
1
1
1
1 (a) The nitro group in organic synthesis, Ed. N. Ono, Wiley-VCH,
2
responding carbonyl compound and N O, oxidative variants are
New York, Chichester, 2001.
known, which nicely parallel the enzymatic reductive equivalent
shown in this study. See:(a) J. U. Nef, Justus Liebigs Ann. Chem.,
1894, 280, 263–342; (b) H. W. Pinnick, Org. React., 1990, 38, 655–792;
(c) R. Ballini and M. Petrini, Tetrahedron, 2004, 60, 1017–1047; (d) L.
Petrus, M. Petrusova, D.-P. Pham-Huu, E. Lattova, B. Pribulova and
J. Turjan, Monatsh. Chem., 2002, 133, 383–392.
2 L. Angermaier and H. Simon, Hoppe-Seyler’s Z. physiol. Chemie,
1
983, 364, 961–975.
3 The bioreduction of oximes by baker’s yeast was reported to yield
amines in modest e.e. and yield, see: D. E. Gibbs and D. Barnes,
Tetrahedron Lett., 1990, 31, 5555–5558.
1
1
1
4 H. Braun, F. P. Schmidtchen, A. Schneider and H. Simon, Tetrahe-
dron, 1991, 47, 3329–3334.
32 K. Francis, B. Russell and G. Gadda, J. Biol. Chem., 2005, 280,
5195–5204; D. J. T. Porter and H. J. Bright, J. Biol. Chem., 1987,
262, 14428–14434; S. C. Daubner, G. Gadda, M. P. Valley and
P. F. Fitzpatrick, Proc. Natl. Acad. Sci. U. S. A., 2002, 99, 2702–
2707.
5 L. Angermaier and H. Simon, Hoppe-Seyler’s Z. physiol. Chemie,
1
983, 364, 1653–1663.
6 (a) A. Mori, I. Ishiyama, H. Akita, K. Suzuki, T. Mitsuoka and T.
Oishi, Xenobiotica, 1990, 20, 629–634; (b) A. Mori, I. Ishiyama, H.
Akita, K. Suzuki, T. Mitsuoka and T. Oishi, Chem. Pharm. Bull.,
33 D. J. T. Porter and H. J. Bright, J. Biol. Chem., 1983, 258, 9913–
9924.
1
990, 38, 3449–3451.
34 C. Breithaupt, R. Kurzbauer, H. Lilie, A. Schaller, J. Strassner, R.
Huber, P. Macheroux and T. Clausen, Proc. Natl. Acad. Sci. U. S. A.,
2006, 103, 14337–14342.
35 K. Kitzing, T. B. Fitzpatrick, C. Wilken, J. Sawa, G. P. Bourenkov,
P. Macheroux and T. Clausen, J. Biol. Chem., 2005, 280, 27904–
27913.
1
7 The bioreduction of nitroalkenes by flavin-dependent enoate reduc-
tases from the old-yellow-enzyme family yields the corresponding
nitroalkanes in high chemical and optical yields, for a review see: R.
Stuermer, B. Hauer, M. Hall and K. Faber, Curr. Opin. Chem. Biol.,
2
007, 11, 201–213.
This journal is © The Royal Society of Chemistry 2010
Green Chem., 2010, 12, 616–619 | 619