Coupling efficiency in light-driven hybrid P450BM3 and CYP119 enzymes
Publication Date
September 2019
Document Type
Article
Publication Title
Archives of Biochemistry and Biophysics
Volume
672
DOI
10.1016/j.abb.2019.108077
First Page
15
Abstract
The light-driven hybrid P450 enzyme approach utilizing the photochemical properties of a covalently attached Ru(II)-diimine photosensitizer was extended to the archaeal Sulfolobus acidocaldarius CYP119 enzyme leading to high photocatalytic activity in the hydroxylation of the chromogenic substrate, 11-nitrophenoxyundecanoic acid. The determined kcat was greater than those reported with various natural redox partners. In addition, the sacrificial electron donor, diethyldithiocarbamate, used in the photocatalytic reaction is shown to play a dual role. It acts as an efficient quencher of the Ru(II) excited state leading to a highly reducing species necessary to inject electrons into the heme. It is also known for its antioxidant properties and is shown herein to be a useful probe to determine coupling efficiency in the light-driven hybrid enzymes.
Keywords
Light-driven process, Uncoupling pathway, Reactive oxygen species, Bacterial P450 enzymes
Recommended Citation
Mallory Kato, Marya Melkie, Jeffrey Li, Bridget Foley, Hoang Truc Nguyen, Liridona Leti, and Lionel Cheruzel. "Coupling efficiency in light-driven hybrid P450BM3 and CYP119 enzymes" Archives of Biochemistry and Biophysics (2019): 15. https://doi.org/10.1016/j.abb.2019.108077
Comments
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