PUBLICATION
Visible light mediated bidirectional control over carbonic anhydrase activity in cells and in vivo using azobenzene sulfonamides
- Authors
- Aggarwal, K., Kuka, T.P., Banik, M., Medellin, B.P., Ngo, C.Q., Xie, D., Fernandes, Y., Dangerfield, T.L., Ye, E., Bouley, B., Johnson, K.A., Zhang, Y.J., Eberhart, J.K., Que, E.L.
- ID
- ZDB-PUB-200708-1
- Date
- 2020
- Source
- Journal of the American Chemical Society 142(34): 14522-14531 (Journal)
- Registered Authors
- Eberhart, Johann
- Keywords
- none
- MeSH Terms
-
- Hydrogen-Ion Concentration
- HeLa Cells
- Molecular Structure
- Molecular Probes/chemical synthesis
- Molecular Probes/chemistry*
- Molecular Docking Simulation
- Light*
- Animals
- Humans
- Sulfonamides/chemical synthesis
- Sulfonamides/chemistry*
- Carbonic Anhydrases/chemistry
- Carbonic Anhydrases/metabolism*
- Zebrafish/embryology
- Azo Compounds/chemical synthesis
- Azo Compounds/chemistry*
- PubMed
- 32623882 Full text @ J. Am. Chem. Soc.
Citation
Aggarwal, K., Kuka, T.P., Banik, M., Medellin, B.P., Ngo, C.Q., Xie, D., Fernandes, Y., Dangerfield, T.L., Ye, E., Bouley, B., Johnson, K.A., Zhang, Y.J., Eberhart, J.K., Que, E.L. (2020) Visible light mediated bidirectional control over carbonic anhydrase activity in cells and in vivo using azobenzene sulfonamides. Journal of the American Chemical Society. 142(34):14522-14531.
Abstract
Two azobenzene sulfonamide 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 nm and 410 nm 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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping