C. Stueckler et al. / Tetrahedron 66 (2010) 663–667
667
4
.10. Determination of enantiomeric excess and absolute
Ehammer, H.; Pointner, E.; Oberdorfer, G.; Gruber, K.; Hauer, B.; Stuermer, R.;
Macheroux, P.; Kroutil, W.; Faber, K. Adv. Synth. Catal. 2008, 350, 411–418.
configuration
1
1. For light-driven cofactor-regeneration see: Massey, V.; Stankovich, M.; Hem-
merich, P. Biochemistry 1978, 17, 1–8; Hollmann, F.; Taglieber, A.; Schulz, F.;
Reetz, M. T. Angew. Chem., Int. Ed. 2007, 46, 2903–2906; Taglieber, A.; Schulz, F.;
Hollmann, F.; Rusek, M.; Reetz, M. T. ChemBioChem 2008, 9, 565–572; for
electrochemical methods see: Hollmann, F.; Hofstetter, K.; Habicher, T.; Hauer,
B.; Schmid, A. J. Am. Chem. Soc. 2005, 127, 6540–6541; Ruinatscha, R.; H o¨ llrigl,
V.; Otto, K.; Schmid, A. Adv. Synth. Catal. 2006, 348, 2015–2026; Hollmann, F.;
Schmid, A. Biocatal. Biotransform. 2004, 22, 63–88; Hollmann, F.; Hofstetter, K.;
Schmid, A. Trends Biotechnol. 2006, 24, 163–171; de Gonzalo, G.; Ottolina, G.;
Carrea, G.; Fraaije, M. W. Chem. Commun. 2005, 3724–3726.
12. Despite the impressive advances in nicotinamide-cofactor recycling using
specific dehydrogenases, such as FDH, GDH, and phosphite-DH, the use of
a single dehydrogenase for concomitant substrate reduction and NADH-re-
cycling via oxidation of 2-propanol is the preferred technique in the asym-
metric bioreduction of ketones catalyzed by ADHs on industrial scale, see Ref. 7.
13. For Old Yellow Enzyme isoenzymes 1–3 see Ref. 3a; for the OYE homolog YqjM
from Bacillus subtilis see: Fitzpatrick, T. B.; Amrhein, N.; Macheroux, P. J. Biol.
Chem. 2003, 278, 19891–19897; for 12-oxophytodienoic acid reductase iso-
enzyme OPR1 see: Straßer, J.; F u¨ rholz, A.; Macheroux, P.; Amrhein, N.; Schaller,
A. J. Biol. Chem. 1999, 274, 35067–35073; for nicotinamide-dependent cyclo-
hexenone reductase (NCR) see Ref. 19; for morphinone reductase (MorR) see:
Messiha, H. L.; Bruce, N. C.; Sattelle, B. M.; Sutcliffe, M. J.; Munro, A. W.;
Scrutton, N. S. J. Biol. Chem. 2005, 280, 27103–27110; for pentyerythritol
tetranitrate reductase (PETNR) see: Khan, H.; Harris, R. J.; Barna, T.; Craig, D. H.;
Bruce, N. C.; Munro, A. W.; Moody, P. C. E.; Scrutton, N. S. J. Biol. Chem. 2002, 277,
The enantiomeric excess of 1a and 3a was determined using
a modified
0
b
-cyclodextrin capillary column (Chiraldex B-TA, 40 m,
ꢁ
.25 mm). Detector temperature 200 C, injector temperature
ꢁ
ꢁ
180 C, split ratio 25:1. Temperature program for 1a: 80 C hold
ꢁ
ꢁ
ꢁ
2
min, 5 C/min to 105 C, 10 C/min, hold 4 min. Retention times:
ꢁ
(R)-1a 6.34 and (S)-1a 6.47 min. Temperature program for 3a: 90 C
ꢁ
ꢁ
ꢁ
ꢁ
hold 4 min, 3 C/min to 115 C, 30 C/min to 180 C. Retention
times: (S)-3b 7.33 min; (R)-3b 7.45 min; The enantiomeric excess of
4
a was determined using a
b-cyclodextrin capillary column (CP-
Chirasil-DEX CB, 25 m, 0.32 mm, 0.25
gram for 4a: 90 C hold 2 min, 4 C/min to 115 C, 20 C/min to
m
m film). Temperature pro-
ꢁ
ꢁ
ꢁ
ꢁ
ꢁ
180 C, hold 2 min. Retention times: (R)-4a 6.42; (S)-4a 6.74 min.
The enantiomeric excess of 8b was determined on HPLC using
n-heptane/i-PrOH 95:5 (isocratic) at 18 C and 1 mL/min. Retention
times: (R)-8b 25.10 min; (S)-8b 29.15 min.
ꢁ
15
Acknowledgements
2
1906–21912; for estrogen-binding protein EBP1 see Ref. 3b. No data are
This work was partially financed by the Fonds zur F o¨ rderung der
wissenschaftlichen Fortschung (FWF, Vienna, project no. 18689);
N.C. Bruce and H. Housden (University of York) are cordially
thanked for providing samples of N-ethylmaleimide-, morphinone-
and PETN-reductase.
available for NemA and OPR3.
14. Kitzing, K.; Fitzpatrick, T. B.; Wilken, C.; Sawa, J.; Bourenkov, G. P.; Macheroux,
P.; Clausen, T. J. Biol. Chem. 2005, 280, 27904–27913.
5. Hall, M.; Stueckler, C.; Hauer, B.; Stuermer, R.; Friedrich, T.; Breuer, M.; Kroutil,
W.; Faber, K. Eur. J. Org. Chem. 2008, 1511–1516.
16. Breithaupt, C.; Strassner, J.; Breitinger, U.; Huber, R.; Macheroux, P.; Schaller, A.;
Clausen, T. Structure 2001, 9, 419–429.
1
1
7. Barna, T.; Messiha, H. L.; Petosa, C.; Bruce, N. C.; Scrutton, N. S.; Moody, P. C. E.
References and notes
J. Biol. Chem. 2002, 277, 30976–30983; Messiha, H. L.; Munroe, A. W.; Bruce, N.
C.; Barsukov, I.; Scrutton, N. S. J. Biol. Chem. 2005, 280, 10695–10709.
18. Williams, R. E.; Rathbone, D. A.; Scrutton, N. S.; Bruce, N. C. Appl. Environ.
Microbiol. 2004, 70, 3566–3574.
19. M u¨ ller, A.; Hauer, B.; Rosche, B. Biotechnol. Bioeng. 2007, 98, 22–29.
20. The slight hydrogen-imbalance is presumed to derive from oxidation of re-
1
. Notable exceptions are the Cannizzaro reaction (2R–CHO/R–CH
2
OHþR–CO
R), Kornblum–DeLaMare rearrangement
C–OH), Meerwein–Ponndorf–Verley/Oppe-
nauer reduction/oxidation (R R COþ2-PrOH4R R CH–OHþacetone), Boudouard
reaction (2CO/CO
þC) and the catalytic disproportionation of toluene
2
H),
Tishchenko reaction (2R–CHO/R–CO
2
0
0
0
0
0
(
R 2CH–O–O–CR
3
/R –CO–R þR’
3
0
0 0
2
duced flavin by O
2 2 2
(producing H O ); see: Hirano, J.; Miyamoto, K.; Ohta, H.
(
2MePh/benzeneþxylene), see: Banks, R. L. J. Mol. Catal. 1980, 8, 269–276;
Appl. Microbiol. Biotechnol. 2008, 80, 71–78; Riebel, B. R.; Gibbs, P. R.; Wellborn,
W. B.; Bommarius, A. S. Adv. Synth. Catal. 2002, 344, 1156–1168.
21. Mueller, N. J.; Stueckler, C.; Hall, M.; Macheroux, P.; Faber, K. Org. Biomol. Chem.
2009, 7, 1115–1119.
22. The (co)-substrate concentrations used in this study were typically 10 mM.
From related studies it can be deduced that increasing of the (co)-substrate
concentrations to ca. 100 mM is feasible.
23. Abramovitz, A. S.; Massey, V. J. Biol. Chem. 1976, 251, 5327–5336.
24. Stark, D.; von Stockar, U. Adv. Biochem. Eng. Biotechnol. 2003, 80, 149–175; Lye,
G. J.; Woodley, J. M. Trends Biotechnol. 1999, 17, 395–402; Etschmann, M. M. W.;
Sell, D.; Schrader, J. Biotechnol. Bioeng. 2005, 92, 624–634.
Abdal Kareem, M. A.; Chand, S.; Mishra, I. M. J. Sci. Ind. Res. 2001, 60, 319–327.
. Finster, K. J. Sulfur Chem. 2008, 29, 281–292; Grinbergs, A. Latvian Chem. J. 2003,
2
3
4
3
, 292; Chem. Abstr. 2004, 140, 419639. It should be noted that in the bio-
chemical literature, ‘disproportionation’ is often denoted as ‘dismutation’.
. (a) Vaz, A. D. N.; Chakraborty, S.; Massey, V. Biochemistry 1995, 34,
4246–4256; (b) Buckman, J.; Miller, S. M. Biochemistry 1998, 37, 14326–14336;
(
c) Karplus, P. A.; Fox, K. M.; Massey, V. FASEB J. 1995, 9, 1518–1526.
. O’Brien, P. J.; Herschlag, D. Chem. Biol. 1999, 6, R91–R105; Kazlauskas, R. J. Curr.
Opin. Chem. Biol. 2005, 9, 195–201; Bornscheuer, U. T.; Kazlauskas, R. J. Angew.
Chem., Int. Ed. 2004, 43, 6032–6040; Hult, K.; Berglund, P. Trends Biotechnol.
2
007, 25, 231–238.
25. Among a series of water-immiscible organic solvents, methyl tert-butyl ether
has been shown to be an ideal co-solvent for OYE-type enoate reductases;
Stueckler, C.; Mueller, N. J.; Winkler, C. K.; Glueck, S. M.; Faber, K., in
preparation.
26. Alphand, V.; Carrea, G.; Wohlgemuth, R.; Furstoss, R.; Woodley, J. M. Trends
Biotechnol. 2003, 21, 318–323; Hilker, I.; Baldwin, C.; Alphand, V.; Furstoss, R.;
Woodley, J.; Wohlgemuth, R. Biotechnol. Bioeng. 2006, 93, 1138–1144; Hilker, I.;
Wohlgemuth, R.; Alphand, V.; Furstoss, R. Biotechnol. Bioeng. 2005, 92, 702–710.
27. Takahashi, O.; Umezawa, J.; Furuhashi, K.; Takagi, M. Tetrahedron Lett. 1989, 30,
1583–1584; Furuhashi, K. In Chirality in Industry; Collins, A. N., Sheldrake, G. N.,
Crosby, J., Eds.; Wiley: New York, NY, 1992; pp 167–186; White, R. F.; Birnbaum, J.;
Meyer, R. T.; ten Broeke, J.; Chemerda, J. M.; Demain, A. L. Appl. Microbiol.1971, 22,
55–60.
5
. (a) Walsh, C. Acc. Chem. Res. 1980, 13, 148–155; Kohli, R. M.; Massey, V. J. Biol.
Chem. 1998, 273, 32763–32770; (b) Williams, R. E.; Bruce, N. C. Microbiology
2
002, 148, 1607–1614.
. Stuermer, R.; Hauer, B.; Hall, M.; Faber, K. Curr. Opin. Chem. Biol. 2007, 11, 201–213.
. Yamamoto, H.; Matsuyama, A. In Biocatalysis in the Pharmaceutical and Bio-
6
7
technology Industry; Patel, R. N., Ed.; CRC: Boca Raton, FL, 2007; pp 623–644;
Wandrey, C. Chem. Rec. 2004, 4, 254–265; Kragl, U.; Vasic-Racki, D.; Wandrey, C.
Indian J. Chem., Sect. B 1993, 32B, 103–117.
. Vrtis, J. M.; White, A. K.; Metcalf, W. W.; van der Donk, W. A. Angew. Chem., Int.
Ed. 2002, 41, 3391–3393; Johannes, T. W.; Woodyer, R. D.; Zhao, H. Biotechnol.
Bioeng. 2006, 96, 18–26; Torres Pazmino, D. E.; Snajdrova, R.; Baas, B.-J.; Ghobrial,
M.; Mihovilovic, M. D.; Fraaije, M. W. Angew. Chem., Int. Ed. 2008, 47, 2275–2278.
. Faber, K. Biotransformations in Organic Chemistry, 5th ed.; Springer: Heidelberg,
8
9
28. Breithaupt, C.; Kurzbauer, R.; Lilie, H.; Schaller, A.; Strassner, J.; Huber, R.;
Macheroux, P.; Clausen, T. Proc. Natl. Acad. Sci. U.S.A. 2006, 103,
14337–14342.
2
004; pp 178–182.
1
0. During the bioreduction of conjugated enones and enals using enoate re-
ductases, carbonyl reduction and substrate-racemisation have frequently been
observed as side reactions. (a) Hall, M.; Stueckler, C.; Kroutil, W.; Macheroux, P.;
Faber, K. Angew. Chem., Int. Ed. 2007, 46, 3934–3937; (b) Hall, M.; Stueckler, C.;
29. French, C. E.; Nicklin, S.; Bruce, N. C. J. Bacteriol. 1996, 178, 6623–6627; Miura, K.;
Tomioka, Y.; Suzuki, H.; Yonezawa, M.; Hishinuma, T.; Mizugaki, M. Biol. Pharm.
Bull. 1997, 20, 110–112; French, C. E.; Bruce, N. C. Biochem. J. 1994, 301, 97–103.