X-RAY CRYSTALLOGRAPHIC STUDIES PROVIDE ADDITIONAL EVIDENCE THAT AN ENZYME-LIKE BINDING POCKET IS CRUCIAL TO THE ENANTIOSELECTIVE DIHYDROXYLATION OF OLEFINS BY OSO4-BIS-CINCHONA ALKALOID COMPLEXES

X-Ray crystallographic analysis on single crystals and H-1 NMR studies in solution of various bis-cinchona alkaloid derivatives reveal a gen eral preference for a conformation which possesses a U-shaped binding pecker with favorable dimensions far the inclusion of olefinic substra tes and the acceleration of face selective dihydroxylation by a proxim ate pentacoordinate OsO4.