Fluorescence excitation spectroscopic characterisation of F2 - colour centers in a LiF crystal

Birkmann, C.; Penzkofer, Alfons; Tsuboi, Taijū

doi:10.1007/s00340-003-1268-6

Cited by 18 publications

(2 citation statements)

References 21 publications

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“…The fluorescence quantum yield ϕ F was calculated using the relation

where the integration runs over the fluorescence emission wavelength region (see Equation (1) above). Fluorescence excitation quantum distributions E ex (λ) were recorded by scanning the fluorescence excitation wavelength over the absorption wavelength region at fixed fluorescence detection wavelengths λ F,det [ 59 ]. Magic angle conditions were applied for the fluorescence recordings (vertical polarized excitation and orientation of the fluorescence detection polarizer at an angle of 54.7° to the vertical [ 60 ]).…”

Section: Methodsmentioning

confidence: 99%

Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor Archon2

Penzkofer

Silapetere

Hegemann

2020

IJMS

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Archon2 is a fluorescent voltage sensor derived from Archaerhodopsin 3 (Arch) of Halorubrum sodomense using robotic multidimensional directed evolution approach. Here we report absorption and emission spectroscopic studies of Archon2 in Tris buffer at pH 8. Absorption cross-section spectra, fluorescence quantum distributions, fluorescence quantum yields, and fluorescence excitation spectra were determined. The thermal stability of Archon2 was studied by long-time attenuation coefficient measurements at room temperature (21 ± 1 °C) and at refrigerator temperature (3 ± 1 °C). The apparent melting temperature was determined by stepwise sample heating up and cooling down (obtained apparent melting temperature: 63 ± 3 °C). In the protein melting process protonated retinal Schiff base (PRSB) with absorption maximum at 586 nm converted to de-protonated retinal Schiff base (RSB) with absorption maximum at 380 nm. Storage of Archon2 at room temperature and refrigerator temperature caused absorption coefficient decrease because of partial protein clustering to aggregates at condensation nuclei and sedimentation. At room temperature an onset of light scattering was observed after two days because of the beginning of protein unfolding. During the period of observation (18 days at 21 °C, 22 days at 3 °C) no change of retinal isomer composition was observed indicating a high potential energy barrier of S0 ground-state isomerization.

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“…The fluorescence quantum yield ϕ F was calculated using the relation

Section: Methodsmentioning

confidence: 99%

Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor Archon2

Penzkofer

Silapetere

Hegemann

2020

IJMS

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“…The fluorescence quantum yield ϕ F was calculated using the relation ϕF=true∫emEF(λ)dλ where the integration runs over the fluorescence emission wavelength region. Fluorescence excitation quantum distributions E ex (λ) were recorded by scanning the fluorescence excitation wavelength over the absorption wavelength region at fixed fluorescence detection wavelengths [82]. Magic angle conditions were applied for the fluorescence recordings (vertical polarized excitation and orientation of the fluorescence detection polarizer at an angle of 54.7° to the vertical [83]).…”

Section: Methodsmentioning

confidence: 99%

Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor QuasAr1

Penzkofer

Silapetere

Hegemann

2019

IJMS

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QuasAr1 is a fluorescent voltage sensor derived from Archaerhodopsin 3 (Arch) of Halorubrum sodomense by directed evolution. Here we report absorption and emission spectroscopic studies of QuasAr1 in Tris buffer at pH 8. Absorption cross-section spectra, fluorescence quantum distributions, fluorescence quantum yields, and fluorescence excitation spectra were determined. The thermal stability of QuasAr1 was studied by long-time attenuation coefficient measurements at room temperature (23 ± 2 °C) and at 2.5 ± 0.5 °C. The apparent melting temperature was determined by stepwise sample heating up and cooling down (obtained apparent melting temperature: 65 ± 3 °C). In the protein melting process the originally present protonated retinal Schiff base (PRSB) with absorption maximum at 580 nm converted to de-protonated retinal Schiff base (RSB) with absorption maximum at 380 nm. Long-time storage of QuasAr1 at temperatures around 2.5 °C and around 23 °C caused gradual protonated retinal Schiff base isomer changes to other isomer conformations, de-protonation to retinal Schiff base isomers, and apoprotein structure changes showing up in ultraviolet absorption increase. Reaction coordinate schemes are presented for the thermal protonated retinal Schiff base isomerizations and deprotonations in parallel with the dynamic apoprotein restructurings.

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Energy transfer in a thin film of TPD fluorescent molecules doped with PtOEP and Ir(ppy)3 phosphorescent molecules

2005

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Fluorescence excitation spectroscopic characterisation of F2 - colour centers in a LiF crystal

Cited by 18 publications

References 21 publications

Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor Archon2

Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor Archon2

Absorption and Emission Spectroscopic Investigation of the Thermal Dynamics of the Archaerhodopsin 3 Based Fluorescent Voltage Sensor QuasAr1

Energy transfer in a thin film of TPD fluorescent molecules doped with PtOEP and Ir(ppy)3 phosphorescent molecules

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