Influence of phosphate ion on the fluorescence of 3-fluorotyrosine

Vdovenko, Sergey I.; Kolycheva, M. T.; Gerus, Igor I.; Kukhar, V. P.

doi:10.1007/bf00805830

Cited by 4 publications

(5 citation statements)

References 7 publications

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“…This was confirmed by measurement of the lifetime as a function of buffer concentration (figure S6 of supplementary information), which demonstrated dynamic quenching, with k q =1.00× 10 9 M −1 s −1 . To our knowledge the quenching of 2AP fluorescence by phosphate buffer has not been reported previously, although phosphate anions have been observed to quench the fluorescence of tryptophan and tyrosine [33][34][35]. Narayanan et al [24] were unaware of the quenching effect of the buffer and erroneously used a literature value of 11.4 ns for τ 0 in calculating k q from K D .…”

Section: Measurements In Phosphate Buffermentioning

confidence: 91%

Dynamic and static quenching of 2-aminopurine fluorescence by the natural DNA nucleotides in solution

Paterson

Arlt

Jones

2020

Methods Appl. Fluoresc.

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2-aminopurine (2AP) is a responsive fluorescent base analogue that is used widely as a probe of the local molecular environment in DNA. The ability of 2AP to report changes in local conformation and base-stacking interactions arises from the efficient quenching of its fluorescence by the natural DNA bases. However, the mechanism of this inter-base quenching remains imperfectly understood. Two previous studies of the collisional quenching of 2AP by the natural bases, in different buffer solutions, showed that dynamic quenching efficiency depends on the identity of the natural base, but disagreed on the relative quenching efficiencies of the bases. We report a comprehensive investigation of inter-base quenching of 2AP by the natural nucleoside monophosphates (NMPs), replicating the buffer conditions used in the previous studies. Using time-resolved fluorescence measurements to distinguish between dynamic and static quenching, we find that the dynamic quenching rate constants of the different bases show a consistent trend across both buffers, and this is in line with a charge-transfer mechanism. Time-resolved measurements also provide insight into static quenching, revealing formation of 2AP-NMP ground-state complexes in which 2AP displays a very short fluorescence lifetime, comparable to that seen in oligonucleotides. In these complexes, the dependence of the rate of quenching on the partner base also supports a charge-transfer mechanism.

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Section: Measurements In Phosphate Buffermentioning

confidence: 91%

Dynamic and static quenching of 2-aminopurine fluorescence by the natural DNA nucleotides in solution

Paterson

Arlt

Jones

2020

Methods Appl. Fluoresc.

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“…26 Å and has been used to study protein folding and structural change, ,,− and protein–protein interactions. − Recently, 3-nitrotyrosine as a fluorescent biosensor for As 3+ , Cl – and I – ions was also reported. , Similarly, it has been shown that 2-nitrotyrosine can act as a FRET quencher to Trp and has been used to study the binding structure of proline-rich peptides and SH3 domain from a yeast myosin . In addition, it has been reported that several fluorotyrosines, such as 2-fluorotyrosine and 3-fluorotyrosine, can tune the fluorescence spectrum of GFP, , and that the fluorescence of 3-fluorotyrosine can be quenched by phosphate …”

Section: Fluorescence Probesmentioning

confidence: 99%

“…Tyrosine-Based UAAs. While a few Tyr-based UAAs are considered fluorescent, such as 3-fluorotyrosine, 320 they have not found extensive spectroscopic utilities as standalone fluorescence reporters. However, various Tyr-based UAAs have been shown to be useful as fluorescence quenchers of other biological fluorophores.…”

Section: Phenylalanine-based Uaasmentioning

confidence: 99%

“…312 In addition, it has been reported that several fluorotyrosines, such as 2-fluorotyrosine and 3-fluorotyrosine, can tune the fluorescence spectrum of GFP, 338,339 and that the fluorescence of 3-fluorotyrosine can be quenched by phosphate. 320…”

Section: Phenylalanine-based Uaasmentioning

confidence: 99%

“…While a few Tyr-based UAAs are considered fluorescent, such as 3-fluorotyrosine, they have not found extensive spectroscopic utilities as stand-alone fluorescence reporters. However, various Tyr-based UAAs have been shown to be useful as fluorescence quenchers of other biological fluorophores. − For example, 3-nitrotyrosine (3NT), which is nonfluorescent, is an efficient quencher of Tyr and Trp fluorescence, because its absorption spectrum is in the wavelength range of 300–450 nm (depending on pH, the λ ab of its neutral form is at 355 nm, whereas the λ ab of its ionized form is at 422 nm) and overlaps with the emission spectra of Tyr and Trp. , The Trp and 3NT fluorophore–quencher pair has an R 0 distance of ca.…”

Section: Fluorescence Probesmentioning

confidence: 99%

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Unnatural Amino Acids for Biological Spectroscopy and Microscopy

Feng,

Wang,

Zhang

et al. 2024

Chem. Rev.

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Due to advances in methods for site-specific incorporation of unnatural amino acids (UAAs) into proteins, a large number of UAAs with tailored chemical and/or physical properties have been developed and used in a wide array of biological applications. In particular, UAAs with specific spectroscopic characteristics can be used as external reporters to produce additional signals, hence increasing the information content obtainable in protein spectroscopic and/or imaging measurements. In this Review, we summarize the progress in the past two decades in the development of such UAAs and their applications in biological spectroscopy and microscopy, with a focus on UAAs that can be used as site-specific vibrational, fluorescence, electron paramagnetic resonance (EPR), or nuclear magnetic resonance (NMR) probes. Wherever applicable, we also discuss future directions.

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