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Published August 31, 2000 | public
Journal Article

Enantiomeric discrimination of Ru-substrates by cytochrome P450_(cam)

Abstract

Molecules with photosensitizers attached to substrates (Wilker et al., Angew. Chem. Int. Ed. 38 (1999) 90–92) or cofactors (Hamachi et al., J. Am. Chem. Soc. 121 (1999) 5500–5506) can rapidly deliver redox equivalents to buried active sites. The structure of cytochrome P450_(cam) (P450) co-crystallized with a prototypal sensitizer-substrate, [Ru-C_9-Ad]Cl_2, has been determined (Dmochowski et al., Proc. Natl. Acad. Sci. USA 96 (1999) 12987–12990); and, in separate UV–vis absorption and time-resolved luminescence experiments, the binding of the Λ and Δ enantiomers of Ru-C_9-Ad to P450 has been measured. The results, K_D(Δ/Λ)∼2, indicate that the bipyridyl ligands of the Λ isomer interact more favorably with hydrophobic residues at the entrance to the substrate channel. We conclude that enantiospecific interactions may be exploited in the design of enzyme-metallosubstrate conjugates.

Additional Information

© 2000 Elsevier Science S.A. Received 7 February 2000, Revised 6 June 2000, Accepted 12 June 2000, Available online 21 September 2000. We thank J.J. Wilker for experimental work, J.H. Dawson, B.R. Crane, E.D.A. Stemp, and A.G. Lappin for helpful discussions, and S.G. Sligar for providing a P450_(cam) vector. I.J.D. is an NIH predoctoral trainee (GM08346). This work was supported by the NIH Metalloprotein Program Project Grant (P01 GM48495) and the National Science Foundation (CHE9807150).

Additional details

Created:
August 21, 2023
Modified:
October 26, 2023