The fine structure of luminescence spectra of azurin

Burstein, Edward A.; Permyakov, Eugene A.; Yashin, V. A.; Burkhanov, S. A.; Agró, Alessandro Finazzi

doi:10.1016/0005-2795(77)90051-4

Cited by 45 publications

(20 citation statements)

References 5 publications

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“…The fluorescence emission from TRP-59 in RNAse-T1 is unusual both for the location of its maximum intensity and the presence of vibrational structure (James et al, 1985). In these respects, the spectrum of RNAse-T1 is comparable to that of azurin which has a single TRP at position 48 (Burstein et al, 1977;Petrich et al, 1987). In both cases, the emission intensity maxima are significantly blue shifted relative to other single TRP proteins, being 318-320 nm in RNAse-T1 and 308 nm in azurin.…”

Section: Emission Spectramentioning

confidence: 93%

Molecular dynamics of tryptophan in ribonuclease-T1. II. Correlations with fluorescence

Axelsen¹,

Prendergast²

1989

Biophysical Journal

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The interactions of tryptophan-59 (TRP-59) and its protein environment in ribonuclease-Tl (RNAse-T1) were examined in a 50-ps molecular dynamics simulation. The simulation used was previously shown to demonstrate a fluorescence anisotropy decay that closely agreed with the experimentally determined limiting anistropy for RNAse-T1 (Axelsen, P. H., C. Haydock, and F. G. Prendergast. 1988. Biophys. J. 54:249-258). Further characterization of TRP-59 side chain dynamics and its protein environment has now been completed and correlated to other photophysical properties of this protein. Angular fluctuations of the side chain occur at rates of 1-10 cycles/ps and are limited to ±0.3 radians in all directions. Side chain motions are primarily limited by nonpolar collisions, although most side atom ring and that the efficiency of a quencher in a protein environment is likely to be a function of molecular symmetry.Biophys. J. Biophysical Society Volume In-plane fluctuations of the long axis; (b) out-of-plane fluctuations of the long axis, (times T, and T2 correspond to Fig. 10; a and b). (c) Out-of-plane fluctuations of the short axis. A 4 J J 198 15 20 25 de) JO FREQUENCY (yc.l"/picos.concD TINE Ipicomoed.)

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Section: Emission Spectramentioning

confidence: 93%

Molecular dynamics of tryptophan in ribonuclease-T1. II. Correlations with fluorescence

Axelsen¹,

Prendergast²

1989

Biophysical Journal

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“…The Trp fluorescence yield gauges conformational changes that result upon adding chemical denaturants, or upon changing the pressure, temperature, or pH. In particular, a dramatic increase in the Trp fluorescence quantum yield is observed when the copper ion is removed from the azurin structure, indicating that the copper ion is quenching this residue (Burstein et al, 1977). Although it was thought that Trp was embedded in a rigid environment in the core of the protein, this view changed after several fluorescence decay components were observed (Hutnik and Szabo, 1989a,b).…”

Section: Introductionmentioning

confidence: 99%

Conformational Changes in Azurin from Pseudomona aeruginosa Induced through Chemical and Physical Protocols

Fuentes

Oyola

Fernández

et al. 2004

Biophysical Journal

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Azurin from Pseudomona aeruginosa is a small copper protein with a single tryptophan (Trp) buried in the structure. The Gibbs free energies associated with the folding of holo azurin, calculated monitoring Trp fluorescence and changes in absorbance on the ligand-to-metal band, are different because these techniques probe their local environments, thereby being able to probe different conformational changes. The presence of an intermediate state was observed during the chemical denaturation of the protein. Upon denaturation, a 30-fold increase is observed in the magnitude of the quenching constant of the tryptophan fluorescence by acrylamide, because this residue becomes more accessible to the quencher. Entrapping the protein in sol-gel materials lowers its stability possibly because the solvation properties of the macromolecule are changed. The thermal denaturation of azurin immobilized in a sol-gel monolith is irreversible, which tends to rule out an aggregation mechanism to account for the irreversibility of the denaturation of the protein free in solution. Unlike the Cu(II) ion, the Gd(III) ion accommodates in site B of azurin with high affinity and the folding free energy of Gd-azurin is larger than that of apo azurin.

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“…Fluorescence measurements were performed with a laboratory-made spectrofluorimeter described earlier [15]. All fluorescence spectra were corrected for the instrumental spectral sensitivity.…”

Section: Methodsmentioning

confidence: 99%

Fluorescence Studies of the Calcium Binding to Whiting (Gadus merlangus) Parvalbumin

Permyakov¹,

Yarmolenko²,

Emelyanenko³

et al. 1980

Eur J Biochem

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The calcium binding by parvalbumin of whiting (Gadus merlangus) has been studied using tryptophanyl fluorescence characteristics. Titration of Ca2+-free parvalbumin with Ca2+ leads to a very pronounced blue shift, narrowing and intensification of the fluorescence spectrum. These spectral changes proceed in two stages reflecting the existence of at least three forms which can be interpreted as (a) the protein without Ca2+, (b) with one Ca2+ and (c) with two bound Ca2+ ions/molecule. The fluorescence of these forms has been identified and the fluorescence spectra measured at varied Ca2+ concentrations were resolved into three components corresponding to these spectral forms.

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The fine structure of luminescence spectra of azurin

Cited by 45 publications

References 5 publications

Molecular dynamics of tryptophan in ribonuclease-T1. II. Correlations with fluorescence

Molecular dynamics of tryptophan in ribonuclease-T1. II. Correlations with fluorescence

Conformational Changes in Azurin from Pseudomona aeruginosa Induced through Chemical and Physical Protocols

Fluorescence Studies of the Calcium Binding to Whiting (Gadus merlangus) Parvalbumin

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