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Redox Control of the P450cam Catalytic Cycle: Effects of Y96F Active Site Mutation and Binding of a Non-Natural Substrate

Published

Author(s)

Vytautas Reipa, M P. Mayhew, Marcia J. Holden, V L. Vilker

Abstract

Spectroelectrochemical measurements are used to demonstrate that active site mutation and binding of a non-natural substrate to P450cam (CYP101) reduces the shift in the redox potential caused by substrate-binding, and thereby results in slower catalytic turnover rate relative to wild-type enzyme with the natural camphor substrate.
Citation
Chemical Communications
Volume
4

Keywords

catalytic turnover rate, spectroelectrochemistry, substrate-binding

Citation

Reipa, V. , Mayhew, M. , Holden, M. and Vilker, V. (2002), Redox Control of the P450cam Catalytic Cycle: Effects of Y96F Active Site Mutation and Binding of a Non-Natural Substrate, Chemical Communications (Accessed March 3, 2024)
Created January 1, 2002, Updated February 19, 2017