Open AccessVisible Light Mediated Bidirectional Control over Carbonic Anhydrase Activity in Cells and in Vivo Using Azobenzenesulfonamides
Author(s) -
Kanchan Aggarwal,
Timothy P. Kuka,
Mandira Banik,
Brenda P. Medellin,
Chinh Q. Ngo,
Da Xie,
Yohaan Fernandes,
Tyler L. Dangerfield,
Elva Ye,
Bailey S. Bouley,
Kenneth A. Johnson,
Yan Jessie Zhang,
Johann K. Eberhart,
Emily L. Que
Publication year - 2020
Publication title -
journal of the american chemical society
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.115
H-Index - 612
eISSN - 1520-5126
pISSN - 0002-7863
DOI - 10.1021/jacs.0c05383
Subject(s) - chemistry , carbonic anhydrase , carbonic anhydrase ii , in vivo , enzyme , molecule , visible spectrum , isomerization , zinc , acetazolamide , biophysics , photochemistry , stereochemistry , biochemistry , catalysis , organic chemistry , medicine , physics , microbiology and biotechnology , optoelectronics , anesthesia , biology
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.