The biotransformation with Beauveria bassiana of 5-dimethylbicyclo[3.2
.1]oct-8-yl-N-phenylcarbamate (11), its anti-isomer 13 and cyclooctyl-
N-phenylcarbamate 31 is described. Based on the observed hydroxylation
positions and on earlier results of oxygenations using this fungus, a
modified distance model for hydroxylations is proposed. The mode of b
inding of the substrate to the enzyme's active site depends on the int
rinsic structure and electronic properties of its electron-rich group.
The regio-and stereochemistry of hydroxylation, however, is determine
d mainly by the structure of the hydrocarbon moiety, namely by a speci
fic gap from the anchoring group. This is represented by a distance of
about 5.5 Angstrom between the oxygen directly attached to the carboc
ycle and hydrogens which potentially can be substituted. (C) 1997 Else
vier Science Ltd.