Asymmetric enzymatic oxidoreductions in organic solvents.
It is now beyond doubt that enzymes can vigorously work even in neat organic solvents containing little or no water. Switching the enzymatic reaction medium from aqueous to nonaqueous can make previously problematic processes feasible through, for example, increased substrate solubility or diminished side reactions. Moreover, when placed in this highly unnatural milieu, enzymes exhibit new and potentially valuable properties, including greater stability, markedly altered selectivity that can be readily controlled by the solvent, and molecular memory. Consequently, novel synthetic and biotechnological opportunities ensue, as illustrated herein by those based on enzymatic oxidoreductions such as the asymmetric peroxidase-catalyzed sulfoxidation of organic sulfides.
Klibanov
Alexander M
AM
Department of Chemistry and Division of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. klibanov@mit.edu
D000426:Alcohol Dehydrogenase / Q000737:chemistry; D004795:Enzyme Stability; D004798:Enzymes / Q000737:chemistry*; D007700:Kinetics; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry; D010544:Peroxidases / Q000737:chemistry; D011487:Protein Conformation; D012997:Solvents / Q000737:chemistry*; D013237:Stereoisomerism; D013379:Substrate Specificity; D013440:Sulfides / Q000737:chemistry
D004798:Enzymes; D012997:Solvents; D013440:Sulfides; C093850:methylphenylsulfide; D010088:Oxidoreductases; D000426:Alcohol Dehydrogenase; D010544:Peroxidases