Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore

The electronic structures of photoactive proteins underlie many natural photoinduced processes. The authors, using UV liquid-microjet photoelectron spectroscopy and quantum chemistry calculations, determine electron detachment energies of the green fluorescent protein chromophore in aqueous solution...

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Main Authors: Omri Tau, Alice Henley, Anton N. Boichenko, Nadezhda N. Kleshchina, River Riley, Bingxing Wang, Danielle Winning, Ross Lewin, Ivan P. Parkin, John M. Ward, Helen C. Hailes, Anastasia V. Bochenkova, Helen H. Fielding
Format: Article
Language:English
Published: Nature Portfolio 2022-01-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-022-28155-5
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author Omri Tau
Alice Henley
Anton N. Boichenko
Nadezhda N. Kleshchina
River Riley
Bingxing Wang
Danielle Winning
Ross Lewin
Ivan P. Parkin
John M. Ward
Helen C. Hailes
Anastasia V. Bochenkova
Helen H. Fielding
author_facet Omri Tau
Alice Henley
Anton N. Boichenko
Nadezhda N. Kleshchina
River Riley
Bingxing Wang
Danielle Winning
Ross Lewin
Ivan P. Parkin
John M. Ward
Helen C. Hailes
Anastasia V. Bochenkova
Helen H. Fielding
author_sort Omri Tau
collection DOAJ
description The electronic structures of photoactive proteins underlie many natural photoinduced processes. The authors, using UV liquid-microjet photoelectron spectroscopy and quantum chemistry calculations, determine electron detachment energies of the green fluorescent protein chromophore in aqueous solution, approaching conditions of the protein environment.
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spelling doaj.art-167b4593b32f448d8dbd2fbeb065156a2022-12-21T23:56:23ZengNature PortfolioNature Communications2041-17232022-01-011311710.1038/s41467-022-28155-5Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophoreOmri Tau0Alice Henley1Anton N. Boichenko2Nadezhda N. Kleshchina3River Riley4Bingxing Wang5Danielle Winning6Ross Lewin7Ivan P. Parkin8John M. Ward9Helen C. Hailes10Anastasia V. Bochenkova11Helen H. Fielding12Department of Chemistry, University College LondonDepartment of Chemistry, University College LondonDepartment of Chemistry, Lomonosov Moscow State UniversityDepartment of Chemistry, Lomonosov Moscow State UniversityDepartment of Chemistry, University College LondonDepartment of Chemistry, University College LondonDepartment of Chemistry, University College LondonDepartment of Chemistry, University College LondonDepartment of Chemistry, University College LondonThe Advanced Centre for Biochemical Engineering, Department of Biochemical Engineering, University College LondonDepartment of Chemistry, University College LondonDepartment of Chemistry, Lomonosov Moscow State UniversityDepartment of Chemistry, University College LondonThe electronic structures of photoactive proteins underlie many natural photoinduced processes. The authors, using UV liquid-microjet photoelectron spectroscopy and quantum chemistry calculations, determine electron detachment energies of the green fluorescent protein chromophore in aqueous solution, approaching conditions of the protein environment.https://doi.org/10.1038/s41467-022-28155-5
spellingShingle Omri Tau
Alice Henley
Anton N. Boichenko
Nadezhda N. Kleshchina
River Riley
Bingxing Wang
Danielle Winning
Ross Lewin
Ivan P. Parkin
John M. Ward
Helen C. Hailes
Anastasia V. Bochenkova
Helen H. Fielding
Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore
Nature Communications
title Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore
title_full Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore
title_fullStr Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore
title_full_unstemmed Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore
title_short Liquid-microjet photoelectron spectroscopy of the green fluorescent protein chromophore
title_sort liquid microjet photoelectron spectroscopy of the green fluorescent protein chromophore
url https://doi.org/10.1038/s41467-022-28155-5
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