We consider nonlinear effects in scattering of light by a periodic structure supporting optical bound states in the continuum. In the spectral vicinity of the bound states the scattered electromagnetic field is resonantly enhanced triggering optical bistability. Using coupled mode approach we derive a nonlinear equation for the amplitude of the resonant mode associated with the bound state. We show that such an equation for the isolated resonance can be easily solved yielding bistable solutions which are in quantitative agreement with the full-wave solutions of Maxwell's equations. The coupled mode approach allowed us to cast the the problem into the form of a driven nonlinear oscillator and analyze the onset of bistability under variation of the incident wave. The results presented drastically simplify the analysis nonlinear Maxwell's equations and, thus, can be instrumental in engineering optical response via bound states in the continuum.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6509346PMC
http://dx.doi.org/10.1038/s41598-019-43672-yDOI Listing

Publication Analysis

Top Keywords

bound states
16
states continuum
12
optical bound
8
coupled mode
8
mode approach
8
maxwell's equations
8
nonlinear
5
bound
5
nonlinear response
4
optical
4

Similar Publications

Electron transfer in polysaccharide monooxygenase catalysis.

Proc Natl Acad Sci U S A

January 2025

California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.

Polysaccharide monooxygenase (PMO) catalysis involves the chemically difficult hydroxylation of unactivated C-H bonds in carbohydrates. The reaction requires reducing equivalents and will utilize either oxygen or hydrogen peroxide as a cosubstrate. Two key mechanistic questions are addressed here: 1) How does the enzyme regulate the timely and tightly controlled electron delivery to the mononuclear copper active site, especially when bound substrate occludes the active site? and 2) How does this electron delivery differ when utilizing oxygen or hydrogen peroxide as a cosubstrate? Using a computational approach, potential paths of electron transfer (ET) to the active site copper ion were identified in a representative AA9 family PMO from (PMO9E).

View Article and Find Full Text PDF

SLC35A2 modulates paramyxovirus fusion events during infection.

PLoS Pathog

January 2025

Department of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri, United States of America.

Paramyxoviruses are significant human and animal pathogens that include mumps virus (MuV), Newcastle disease virus (NDV) and the murine parainfluenza virus Sendai (SeV). Despite their importance, few host factors implicated in paramyxovirus infection are known. Using a recombinant SeV expressing destabilized eGFP (rSeVCdseGFP) in a loss-of-function CRISPR screen, we identified the CMP-sialic acid transporter (CST) gene SLC35A1 and the UDP-galactose transporter (UGT) gene SLC35A2 as essential for paramyxovirus infection.

View Article and Find Full Text PDF

Cellulase was effectively immobilized onto an epoxy-bound chitosan-modified zinc metal-organic framework (epoxy/ZIF-8/CS/cellulase) support, yielding a conjugation rate of 0.64 ± 0.02 mg/cm2 and retaining 80.

View Article and Find Full Text PDF

Psoriasis is an inflammatory dermatosis that features overproliferation and inflammatory reaction of keratinocytes. A study reported that IL-22 is involved in the pathogenesis of psoriasis by mediating miR-124 to regulate the expression of fibroblast growth factor receptor 2 in keratinocytes. A microRNA may target multiple target genes.

View Article and Find Full Text PDF

Unveiling the enzymatic pathway of UMG-SP2 urethanase: insights into polyurethane degradation at the atomic level.

Chem Sci

December 2024

LAQV@REQUIMTE, Departamento de Química e Bioquímica, Faculdade de Ciências, Universidade do Porto Rua do Campo Alegre s/n 4169-007 Porto Portugal

The recently discovered metagenomic urethanases UMG-SP1, UMG-SP2, and UMG-SP3 have emerged as promising tools to establish a bio-based recycling approach for polyurethane (PU) waste. These enzymes are capable of hydrolyzing urethane bonds in low molecular weight dicarbamates as well as in thermoplastic PU and the amide bond in polyamide employing a Ser-Ser -Lys triad for catalysis, similar to members of the amidase signature protein superfamily. Understanding the catalytic mechanism of these urethanases is crucial for enhancing their enzymatic activity and improving PU bio-recycling processes.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!