Visible Light Mediated Bidirectional Control over Carbonic Anhydrase Activity in Cells and <i>in Vivo</i> Using Azobenzenesulfonamides

Abstract

Two azobenzenesulfonamide molecules with thermally stable <i>cis</i> configurations resulting from fluorination of positions <i>ortho</i> to the azo group are reported that can differentially regulate the activity of carbonic anhydrase in the <i>trans</i> and <i>cis</i> configurations. These fluorinated probes each use two distinct visible wavelengths (520 and 410 or 460 nm) for isomerization with high photoconversion efficiency. Correspondingly, the <i>cis</i> 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 <i>in vivo</i> in zebrafish during embryo development.