초록
<P>In the field of industrial biocatalysis, formate dehydrogenase (FDH) is well established, in particular for its broad application in cofactor regeneration. Further applications have been limited by the enzyme's narrow range of substrates. These restrictions have been overcome now by the finding, that the enzyme is capable of selectively cleaving formic acid esters to the respective alcohol. Five homologous alkyl formates and phenyl formate as an aromatic ester were converted quantitatively by FDH from <I>Candida boidinii</I> in a batch reaction within 3 to 5 h. The substrates were turned irreversibly into carbon dioxide and the respective alcohol through hydride abstraction from the formyl group with full conversion. The mechanism shows parallels to hydrolysis reactions of the A<SUB>AC</SUB>1-type. K<SUB>M</SUB>-values and reactions rates of the tested formic acid esters display a tendency to higher conversion rates with increasing chain length. FDH emerged to be a superior deformylation catalyst compared to hydrolases as well as classical catalysts, as was shown by the selective deformylation of 1-acetoxy-4-formoxy butane (92%) and 1,3-bis(3-formoxypropyl)tetramethyldisiloxane. In particular its capability to distinguish between formic acid esters and non-formic acid esters renders the method particularly suitable for protective group chemistry. Furthermore the completeness of deformylation allows for converting substrates highly incompatible with aqueous media like siloxanes within a few hours.</P> <P>Graphic Abstract</P><P>Formate dehydrogenase affords selective deprotection of formylated alcohols while acylated alcohols remain unaffected.<BR><IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c1ob06064c'><BR></P>