Use of lipoxygenase and peroxidase for selective catalyses in the organic synthesis
Project management at the University of Würzburg:
In the lipoxygenase (LOX) oriented part, the potential of the soybean isoenzyme L-1 for the regio- and enantioselective dioxygenation of phenolic 1,4-(Z,Z)-alkadienes and -alkatrienes was studied. Using various synthesized substrates and the natural cardanoldiene selective LOX catalysis was realized. The length of the alkadiene(triene) residue was found to be important for the effectivity; highest kcat values were obtained for substrates with a linoleic acid-analogous side chain. Even arylalkenones, which a priori are not in agreement with the established catalytic LOX mechanism, were transformed by L-1. Using curcumin as substrate, three novel bicyclic products were described for the first time.
In the peroxidase (POD) oriented part, the potential of horseradish peroxidase (HRP) for the enantioselective reduction of racemic alkyl aryl hydroperoxides was studied. The results of kinetic resolutions showed that HRP reduced sterically unhindered hydroperoxides with high enantioselectivity, resulting in the formation of optically active hydroperoxides and alcohols with enantiomeric excesses from 80-100%. The chiral recognition was limited in case of sterical hindering in the alkyl chain and with alpha-functionalized hydroperoxides. Tertiary hydroperoxides were not accepted as substrates. In addition, HRP was found to be an effective, but unselective catalyst for biaryl synthesis.
In all the studies chromatographic methods and the exciton coupled circular dichroism (ECCD) technique were used for the stereocontrol and the determination of absolute configurations.
Exciton circular dichroism
from 01.1996 to 12.1998
DFG ,Granting date: 01.10.1995
- W. Adam, U.Hoch, H.U. Humpf, C.R. Saha-Möller, P. Schreier.
(1996). Horseradish peroxidase (HRP) catalyzed enantioselective reduction of racemic homoallylic alcohols: a novel enzymatic method for the preparation of optically active unsaturated diols and hydroperoxy alcohols. (monograph)
- O. Gimple, P. Schreier, H.U. Humpf.
(1997). A new exciton-coupled circular dichroism method for assigning the absolute configuration in acyclic and alpha- and beta-hydroxy carboxylic acids. (monograph)
- U. Hoch, W. Adam, R. Fell, C.R. Saha-Möller, P. Schreier.
(1997). Horseradish peroxidase - a biocatalyst for the one-pot synthesis of enantiomerically pure hydroperoxides and alcohols. (monograph)
- U. Hoch, H.U. Humpf, P. Schreier, C.R. Saha-Möller, W. Adam.
(1997). Configurational assignment of optically active hydroperoxy homoallylic alcohols and the corresponding diols by circular dichroism and multidimensional chromatography. (monograph)
- C. Schneider, P. Schreier, H.U. Humpf.
(1997). Exciton-coupled circular dichroism (ECCD) in acyclic hydroxylated dienes: A sensitive method for the direct sterochemical assignment of lipoxygenase products. (monograph)
- M.M. Schmitt, E. Schüler, M. Braun, D. Häring, P. Schreier.
(1998). Horseradish peroxidase: An effective but unselective biocatalyst for biaryl synthesis. (monograph)
- M. Roth, B. Gutsche, M. Herderich, H.U. Humpf, P. Schreier.
(1998). Dioxygenation of long-chain alkadienyl(trienyl)phenols by soybean lipoxygenase. (monograph)
- C. Schneider, A. Amberg, J. Feurle, A. Roß, M. Roth, G. Toth, P. Schreier.
(1998). 2-[(4''-Hydroxy-3'-methoxy)-phenoxy]-4-(4''-hydroxy-3''-methoxy-phenyl)-8-hydroxy-6-oxo-3-oxo-3-oxabicyclo[3.3.0]-7-octene: Unusual product of the soybean lipoxygenase-catalyzed oxygenmation of curcumin. (monograph)
- W. Adam, M. Lazarus, C.R. Saha-Möller, P. Schreier.
(1999). Biocatalytic synthesis of optically active alpha-oxyfunctionalized carbonyl compounds. (monograph)
- G. Toth, M. Roth, B. Weckerle, P. Schreier.
(2000). Structural elucidation of two novel products from the soybean lipoxygenase-catalyzed dioxygenation of curcumin. (monograph)