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Enhancing Electron Donor-Acceptor Complex Photoactivation with a Stable Perylene Diimide Metal-Organic Framework.
J Am Chem Soc
January 2025
Department of Chemistry, The University of Hong Kong, Hong Kong 999077, P. R. China.
Electron donor-acceptor complexes are commonly employed to facilitate photoinduced radical-mediated organic reactions. However, achieving these photochemical processes with catalytic amounts of donors or acceptors can be challenging, especially when aiming to reduce catalyst loadings. Herein, we have unveiled a framework-based heterogenization approach that significantly enhances the photoredox activity of perylene diimide species in radical addition reactions with alkyl silicates by promoting faster and more efficient electron donor-acceptor complex formation.
View Article and Find Full Text PDFUnveiling Heavier Dihydropyridine Chalcogenol Esters in Metallaphotoredox Catalyst-Enabled Regioselective Hydrothio(seleno)carbonylation.
Org Lett
January 2025
School of Chemistry, Indian Institute of Science Education and Research Thiruvananthapuram, Thiruvananthapuram 695551, Kerala, India.
Herein, aromaticity-driven thio(seleno)ester group transfer from novel 1,4-dihydropyridine thio(seleno)esters to alkene feedstocks is disclosed by merging palladium and photoredox catalysis. In this process, photoactivation of dihydropyridine thio(seleno)esters is integrated with regioselective hydrometalation of alkenes, avoiding photoinduced Pd-C bond homolysis of organopalladium intermediates. Additionally, a regioselective hydroselenocarbonylation of an alkene is accomplished for the first time using a bench-stable selenoester reagent.
View Article and Find Full Text PDFProbing the Signal Transduction Mechanism of the Light-Activated Adenylate Cyclase OaPAC Using Unnatural Amino Acid Mutagenesis.
ACS Chem Biol
January 2025
Department of Chemistry, Stony Brook University, Stony Brook, New York 11794-3400, United States.
OaPAC, the photoactivated adenylyl cyclase from , is composed of a blue light using FAD (BLUF) domain fused to an adenylate cyclase (AC) domain. Since both the BLUF and AC domains are part of the same protein, OaPAC is a model for understanding how the ultrafast modulation of the chromophore binding pocket caused by photoexcitation results in the activation of the output domain on the μs-s time scale. In the present work, we use unnatural amino acid mutagenesis to identify specific sites in the protein that are involved in transducing the signal from the FAD binding site to the ATP binding site.
View Article and Find Full Text PDFDeveloping photoactivated artificial enzymes for sustainable fuel production.
Curr Opin Chem Biol
December 2024
Department of Chemistry and Biochemistry, The Ohio State University, Columbus, OH 43210, USA; Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90095, USA. Electronic address:
Enzymes catalyze molecular reactions with remarkable efficiency and selectivity under mild conditions. Photoactivated enzymes make use of a light-absorbing chromophore to drive chemical transformations, ideally using sunlight as an energy source. The direct attachment of a chromophore to native enzymes is advantageous, as information on the underlying catalytic mechanisms can be obtained.
View Article and Find Full Text PDFThe LOV2 domain is commonly harnessed as a source of light-based regulation in engineered optogenetic switches. In prior work, we used LOV2 to create a light-regulated Dihydrofolate Reductase (DHFR) enzyme and showed that structurally disperse mutations in DHFR were able to tune the allosteric response to light. However, it remained unclear how light allosterically activates DHFR, and how disperse mutations modulate the allosteric effect.
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