Turning the challenge of quantum biology on its head: biological control of quantum optical systems. (24th April 2019)
- Record Type:
- Journal Article
- Title:
- Turning the challenge of quantum biology on its head: biological control of quantum optical systems. (24th April 2019)
- Main Title:
- Turning the challenge of quantum biology on its head: biological control of quantum optical systems
- Authors:
- Lishchuk, Anna
Vasilev, Cvetelin
Johnson, Matthew P.
Hunter, C. Neil
Törmä, Päivi
Leggett, Graham J. - Abstract:
- Abstract : Strong coupling between plasmon modes and chlorins in synthetic light-harvesting maquette proteins yields hybrid light-matter states (plexcitons) whose energies are controlled by design of protein structure, enabling the creation of new states not seen under weak coupling. Abstract : When light-harvesting complex II (LHCII), isolated from spinach, is adsorbed onto arrays of gold nanostructures formed by interferometric lithography, a pronounced splitting of the plasmon band is observed that is attributable to strong coupling of the localised surface plasmon resonance to excitons in the pigment–protein complex. The system is modelled as coupled harmonic oscillators, yielding an exciton energy of 2.24 ± 0.02 eV. Analysis of dispersion curves yields a Rabi energy of 0.25 eV. Extinction spectra of the strongly coupled system yield a resonance at 1.43 eV that varies as a function of the density of nanostructures in the array. The enhanced intensity of this feature is attributed to strong plasmon–exciton coupling. Comparison of data for a large number of light-harvesting complexes indicates that by control of the protein structure and/or pigment compliment it is possible to manipulate the strength of plasmon–exciton coupling. In strongly coupled systems, ultra-fast exchange of energy occurs between pigment molecules: coherent coupling between non-local excitons can be manipulated via selection of the protein structure enabling the observation of transitions that are notAbstract : Strong coupling between plasmon modes and chlorins in synthetic light-harvesting maquette proteins yields hybrid light-matter states (plexcitons) whose energies are controlled by design of protein structure, enabling the creation of new states not seen under weak coupling. Abstract : When light-harvesting complex II (LHCII), isolated from spinach, is adsorbed onto arrays of gold nanostructures formed by interferometric lithography, a pronounced splitting of the plasmon band is observed that is attributable to strong coupling of the localised surface plasmon resonance to excitons in the pigment–protein complex. The system is modelled as coupled harmonic oscillators, yielding an exciton energy of 2.24 ± 0.02 eV. Analysis of dispersion curves yields a Rabi energy of 0.25 eV. Extinction spectra of the strongly coupled system yield a resonance at 1.43 eV that varies as a function of the density of nanostructures in the array. The enhanced intensity of this feature is attributed to strong plasmon–exciton coupling. Comparison of data for a large number of light-harvesting complexes indicates that by control of the protein structure and/or pigment compliment it is possible to manipulate the strength of plasmon–exciton coupling. In strongly coupled systems, ultra-fast exchange of energy occurs between pigment molecules: coherent coupling between non-local excitons can be manipulated via selection of the protein structure enabling the observation of transitions that are not seen in the weak coupling regime. Synthetic biology thus provides a means to control quantum-optical interactions in the strong coupling regime. … (more)
- Is Part Of:
- Faraday discussions. Volume 216(2019)
- Journal:
- Faraday discussions
- Issue:
- Volume 216(2019)
- Issue Display:
- Volume 216, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 216
- Issue:
- 2019
- Issue Sort Value:
- 2019-0216-2019-0000
- Page Start:
- 57
- Page End:
- 71
- Publication Date:
- 2019-04-24
- Subjects:
- Chemistry -- Periodicals
Metallurgy -- Periodicals
Electrochemistry -- Periodicals
540 - Journal URLs:
- http://pubs.rsc.org/en/journals/journalissues/fd#!issueid=fd016192&type=current&issnprint=1359-6640 ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c8fd00241j ↗
- Languages:
- English
- ISSNs:
- 1359-6640
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3866.900000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 11070.xml