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 April 19, 2024)
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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)
, , ,
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
Pub Type
Journals
Keywords
catalytic turnover rate, spectroelectrochemistry, substrate-binding
Citation
Created January 1, 2002, Updated February 19, 2017