No abstract

No abstract

No abstract

shows a weak signal of =+l mdeg at 552 nm due to the isomer, which indicates preferential binding to the protein by the isomer.The experiment is difficult and the magnitude of the result is at the limits of detection; however, a similar result was obtained that indicated the selective binding of A-[Co(ox)3]3_ to the oxidized protein in a previous study.15 Like the stereoselective electrontransfer experiment, interpretation of this chiral recognition of [Cr(ox)3]* 3" by cytochrome c is difficult. Although the number of strong interactions between the protein and [Cr(ox)3]3" appears limited, the stereoselectivity observed is the weighted average of all the interactions that take place. Thus, a highly stereoselective but minor interaction can make a larger contribution to the overall value than a dominant, less selective interaction. Nevertheless, it is of considerable interest to note that the chiral recognition in the binding interaction favors the same A isomer as chiral induction in the electron-transfer process.Acknowledgment. We wish to acknowledge Mr. T. P. Shields for preliminary studies on this system and the generous support of this work by the National Science Foundation (Grant Nos. CHE 87-02012 to A.G.L. and CHE 89-21985 to J.R.P.).

No abstract