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- W3039270016 abstract "Two azobenzenesulfonamide molecules with thermally stable cis configurations resulting from fluorination of positions ortho to the azo group are reported that can differentially regulate the activity of carbonic anhydrase in the trans and cis configurations. These fluorinated probes each use two distinct visible wavelengths (520 and 410 or 460 nm) for isomerization with high photoconversion efficiency. Correspondingly, the cis isomer of these systems is highly stable and persistent (as evidenced by structural studies in solid and solution state), permitting regulation of metalloenzyme activity without continuous irradiation. Herein, we use these probes to demonstrate the visible light mediated bidirectional control over the activity of zinc-dependent carbonic anhydrase in solution as an isolated protein, in intact live cells and in vivo in zebrafish during embryo development." @default.
- W3039270016 created "2020-07-10" @default.
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- W3039270016 date "2020-07-04" @default.
- W3039270016 modified "2023-10-15" @default.
- W3039270016 title "Visible Light Mediated Bidirectional Control over Carbonic Anhydrase Activity in Cells and <i>in Vivo</i> Using Azobenzenesulfonamides" @default.
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- W3039270016 doi "https://doi.org/10.1021/jacs.0c05383" @default.
- W3039270016 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8063266" @default.
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