Fate of the fluorescent state of p-amido analogue of green fluorescence protein chromophore

Yi Hui Chen, Robert Sung, Kuang-Sen Sung

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

When the wild-type green fluorescent protein (wtGFP) chromophore, p-hydroxybenzylidene-imidazolinone (p-HBDI), was modified into various analogues, its fluorescent state and relaxation pathways were also changed dramatically. In contrast to p-HBDI and its various analogues, such as the o-hydroxy analogue (o-HBDI), the o-sulfonamide analogue (o-TsABDI), the p-sulfonamide analogue (p-TsABDI) and the p-amino analogue (p-ABDI), the p-amido analogue (p-AABDI) of wtGFP chromophore displays single fluorescence and its electronic absorption and fluorescence emission do not involve a charge transfer. Its ground-state N–H acid strength (pKa) is 19.6 in DMSO, which is not very acidic, so, unlike p-TsABDI, p-AABDI does not undergo an excited-state proton transfer. Its S1 excited state decays mainly along τ torsion through the S1/S0 conical intersection with a barrier of 2.8 kcal/mol. This was confirmed by the cis-trans photoisomerization experiment, in which 47% of cis-p-AABDI was converted to its trans-form right after 20 min irradiation with 350 nm UV light.

Original languageEnglish
Pages (from-to)446-450
Number of pages5
JournalJournal of Luminescence
Volume213
DOIs
Publication statusPublished - 2019 Sep 1

Fingerprint

Sulfonamides
Chromophores
Green Fluorescent Proteins
Excited states
chromophores
Fluorescence
analogs
proteins
Photoisomerization
fluorescence
Proton transfer
Ultraviolet Rays
Dimethyl Sulfoxide
Ultraviolet radiation
Torsional stress
Ground state
Protons
Charge transfer
Proteins
Irradiation

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Atomic and Molecular Physics, and Optics
  • Chemistry(all)
  • Biochemistry
  • Condensed Matter Physics

Cite this

@article{8223ed14b3e0483bb2df49ebe61a6412,
title = "Fate of the fluorescent state of p-amido analogue of green fluorescence protein chromophore",
abstract = "When the wild-type green fluorescent protein (wtGFP) chromophore, p-hydroxybenzylidene-imidazolinone (p-HBDI), was modified into various analogues, its fluorescent state and relaxation pathways were also changed dramatically. In contrast to p-HBDI and its various analogues, such as the o-hydroxy analogue (o-HBDI), the o-sulfonamide analogue (o-TsABDI), the p-sulfonamide analogue (p-TsABDI) and the p-amino analogue (p-ABDI), the p-amido analogue (p-AABDI) of wtGFP chromophore displays single fluorescence and its electronic absorption and fluorescence emission do not involve a charge transfer. Its ground-state N–H acid strength (pKa) is 19.6 in DMSO, which is not very acidic, so, unlike p-TsABDI, p-AABDI does not undergo an excited-state proton transfer. Its S1 excited state decays mainly along τ torsion through the S1/S0 conical intersection with a barrier of 2.8 kcal/mol. This was confirmed by the cis-trans photoisomerization experiment, in which 47{\%} of cis-p-AABDI was converted to its trans-form right after 20 min irradiation with 350 nm UV light.",
author = "Chen, {Yi Hui} and Robert Sung and Kuang-Sen Sung",
year = "2019",
month = "9",
day = "1",
doi = "10.1016/j.jlumin.2019.05.054",
language = "English",
volume = "213",
pages = "446--450",
journal = "Journal of Luminescence",
issn = "0022-2313",
publisher = "Elsevier",

}

Fate of the fluorescent state of p-amido analogue of green fluorescence protein chromophore. / Chen, Yi Hui; Sung, Robert; Sung, Kuang-Sen.

In: Journal of Luminescence, Vol. 213, 01.09.2019, p. 446-450.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Fate of the fluorescent state of p-amido analogue of green fluorescence protein chromophore

AU - Chen, Yi Hui

AU - Sung, Robert

AU - Sung, Kuang-Sen

PY - 2019/9/1

Y1 - 2019/9/1

N2 - When the wild-type green fluorescent protein (wtGFP) chromophore, p-hydroxybenzylidene-imidazolinone (p-HBDI), was modified into various analogues, its fluorescent state and relaxation pathways were also changed dramatically. In contrast to p-HBDI and its various analogues, such as the o-hydroxy analogue (o-HBDI), the o-sulfonamide analogue (o-TsABDI), the p-sulfonamide analogue (p-TsABDI) and the p-amino analogue (p-ABDI), the p-amido analogue (p-AABDI) of wtGFP chromophore displays single fluorescence and its electronic absorption and fluorescence emission do not involve a charge transfer. Its ground-state N–H acid strength (pKa) is 19.6 in DMSO, which is not very acidic, so, unlike p-TsABDI, p-AABDI does not undergo an excited-state proton transfer. Its S1 excited state decays mainly along τ torsion through the S1/S0 conical intersection with a barrier of 2.8 kcal/mol. This was confirmed by the cis-trans photoisomerization experiment, in which 47% of cis-p-AABDI was converted to its trans-form right after 20 min irradiation with 350 nm UV light.

AB - When the wild-type green fluorescent protein (wtGFP) chromophore, p-hydroxybenzylidene-imidazolinone (p-HBDI), was modified into various analogues, its fluorescent state and relaxation pathways were also changed dramatically. In contrast to p-HBDI and its various analogues, such as the o-hydroxy analogue (o-HBDI), the o-sulfonamide analogue (o-TsABDI), the p-sulfonamide analogue (p-TsABDI) and the p-amino analogue (p-ABDI), the p-amido analogue (p-AABDI) of wtGFP chromophore displays single fluorescence and its electronic absorption and fluorescence emission do not involve a charge transfer. Its ground-state N–H acid strength (pKa) is 19.6 in DMSO, which is not very acidic, so, unlike p-TsABDI, p-AABDI does not undergo an excited-state proton transfer. Its S1 excited state decays mainly along τ torsion through the S1/S0 conical intersection with a barrier of 2.8 kcal/mol. This was confirmed by the cis-trans photoisomerization experiment, in which 47% of cis-p-AABDI was converted to its trans-form right after 20 min irradiation with 350 nm UV light.

UR - http://www.scopus.com/inward/record.url?scp=85066290593&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85066290593&partnerID=8YFLogxK

U2 - 10.1016/j.jlumin.2019.05.054

DO - 10.1016/j.jlumin.2019.05.054

M3 - Article

AN - SCOPUS:85066290593

VL - 213

SP - 446

EP - 450

JO - Journal of Luminescence

JF - Journal of Luminescence

SN - 0022-2313

ER -