Tryptophan fluorescence monitors structural changes accompanying signalling state formation in the photocycle of photoactive yellow protein

2004 ◽  
Vol 3 (6) ◽  
pp. 531 ◽  
Author(s):  
Thomas Gensch ◽  
Johnny Hendriks ◽  
Klaas J. Hellingwerf
Keyword(s):  
State Formation ◽  
Structural Changes ◽  
Tryptophan Fluorescence ◽  
Photoactive Yellow Protein

Binding of Hydrogen-Citrate to Photoactive Yellow Protein Is Affected by the Structural Changes Related to Signaling State Formation

2012 ◽  
Vol 116 (44) ◽  
pp. 13172-13182 ◽  
Author(s):  
Marijke Hospes ◽  
Johannes H. Ippel ◽  
Rolf Boelens ◽  
Klaas J. Hellingwerf ◽  
Johnny Hendriks
Keyword(s):  
State Formation ◽  
Structural Changes ◽  
Photoactive Yellow Protein

scholarly journals Effect of cosolvents (polyols) on structural and foaming properties of soy protein isolate  

2017 ◽  
Vol 35 (No. 1) ◽  
pp. 57-66 ◽  
Author(s):  
Pan Mingzhe ◽  
Meng Xianjun ◽  
Jiang Lianzhou ◽  
Yu Dianyu ◽  
Liu Tianyi
Keyword(s):  
Soy Protein ◽  
Structural Changes ◽  
Foam Stability ◽  
Soy Protein Isolate ◽  
Tryptophan Fluorescence ◽  
Surface Hydrophobicity ◽  
Cd Spectroscopy ◽  
Protein Isolate ◽  
Foaming Properties ◽  
Intrinsic Tryptophan Fluorescence

Effect of polyols (mannitol, sorbitol, and xylitol) at three concentrations (5, 10, and 15% w/w) on the structure of soy protein isolates (SPI) was investigated. Changes in foaming properties of SPI were then examined with the addition of polyols at different concentrations. The interactions between SPI and polyols resulted in a substantial decrease in protein surface hydrophobicity and intrinsic tryptophan fluorescence intensity, along with the covering of tyrosine. Furthermore, circular dichroism (CD) spectroscopy of SPI suggested that a more ordered and compact conformation was induced by polyols. Consequently, these structural changes led to lower foamability of SPI. An increase in the viscosity of SPI suspension seemed to be advantageous for improving the foam stability of SPI.

scholarly journals Comparison of the Photochemical Reaction of Photoactive Yellow Protein in Crystal with Reaction in Solution1

2003 ◽  
Vol 17 (2-3) ◽  
pp. 345-353 ◽  
Author(s):  
Eriko Mano ◽  
Hironari Kamikubo ◽  
Yasushi Imamoto ◽  
Mikio Kataoka
Keyword(s):  
Photochemical Reaction ◽  
Structural Changes ◽  
Spectroscopic Studies ◽  
Crystalline Lattice ◽  
Photoactive Yellow Protein ◽  
X Ray ◽  
X Ray Crystallography ◽  
Solution Condition ◽  
Active Intermediate ◽  
Ectothiorhodospira Halophila

Photoactive yellow protein (PYP) is a photoreceptor protein for the negative phototaxis ofEctothiorhodospira halophila. The crystal structures of several photo‒intermediates have been revealed by X-ray crystallography. In the crystal structure of the active intermediate, PYPM, no significant structural changes were observed except for the vicinity of the chromophore. On the contrary, spectroscopic studies with solution condition demonstrated that global structural changes occur during the photo‒cycle. In order to reveal the origin of the discrepancies, we measured the reaction kinetics upon illumination under crystal condition and to compare them with those observed under solution condition. The reactive portion decreases with the increase of crystallinity. The rate constant of PYPMdecay also decreases with the increase of crystallinity. These results suggest two possibilities: (1) PYP in crystal does not react by the illumination; (2) the photoreaction rate is highly accelerated in crystal. Consequently, the photoreaction in crystal is considered to be highly influenced by the force constraint from crystalline lattice.

scholarly journals Chromophore Conformation and the Evolution of Tertiary Structural Changes in Photoactive Yellow Protein

Structure ◽  
2004 ◽  
Vol 12 (6) ◽  
pp. 1039-1045 ◽  
Author(s):  
Spencer Anderson ◽  
Vukica Srajer ◽  
Reinhard Pahl ◽  
Sudarshan Rajagopal ◽  
Friedrich Schotte ◽  
...  
Keyword(s):  
Structural Changes ◽  
Photoactive Yellow Protein

Time-Resolved Single Tryptophan Fluorescence in Photoactive Yellow Protein Monitors Changes in the Chromophore Structure during the Photocycle via Energy Transfer†

Biochemistry ◽  
2005 ◽  
Vol 44 (51) ◽  
pp. 16804-16816 ◽  
Author(s):  
Harald Otto ◽  
Daniel Hoersch ◽  
Terry E. Meyer ◽  
Michael A. Cusanovich ◽  
Maarten P. Heyn
Keyword(s):  
Energy Transfer ◽  
Tryptophan Fluorescence ◽  
Photoactive Yellow Protein ◽  
Time Resolved

scholarly journals Evidence for a major structural change in Escherichia coli chorismate synthase induced by flavin and substrate binding

1998 ◽  
Vol 335 (2) ◽  
pp. 319-327 ◽  
Author(s):  
Peter MACHEROUX ◽  
Ernst SCHÖNBRUNN ◽  
Dmitri I. SVERGUN ◽  
Vladimir V. VOLKOV ◽  
Michel H. J. KOCH ◽  
...  
Keyword(s):  
Ternary Complex ◽  
Structural Changes ◽  
Tertiary Structure ◽  
Tryptophan Fluorescence ◽  
Cd Spectroscopy ◽  
Scattering Data ◽  
Discrete State ◽  
Chorismate Synthase ◽  
X Ray Scattering ◽  
Ft Ir

Chorismate synthase (EC 4.6.1.4) catalyses the conversion of 5-enolpyruvylshikimate 3-phosphate (EPSP) into chorismate, and requires reduced FMN as a cofactor. The enzyme can bind first oxidized FMN and then EPSP to form a stable ternary complex which does not undergo turnover. This complex can be considered to be a model of the ternary complex between enzyme, EPSP and reduced FMN immediately before catalysis commences. It is shown that the binding of oxidized FMN and EPSP to chorismate synthase affects the properties and structure of the protein. Changes in small-angle X-ray scattering data, decreased susceptibility to tryptic digestion and altered Fourier-transform (FT)-IR spectra provide the first strong evidence for major structural changes in the protein. The tetrameric enzyme undergoes correlated screw movements leading to a more overall compact shape, with no change in oligomerization state. The changes in the FT-IR spectrum appear to reflect changes in the environment of the secondary-structural elements rather than alterations in their distribution, because the far-UV CD spectrum changes very little. Changes in the mobility of the protein during non-denaturing PAGE indicate that the ternary complex may exhibit less conformational flexibility than the apoprotein. Increased enzyme solubility and decreased tryptophan fluorescence are discussed in the light of the observed structural changes. The secondary structure of the enzyme was investigated using far-UV CD spectroscopy, and the tertiary structure was predicted to be an α–β-barrel using discrete state-space modelling.

Photo-isomerization of the isolated photoactive yellow protein chromophore: What comes before the primary step?

2021 ◽  
Author(s):  
Cate S Anstöter ◽  
Basile Curchod ◽  
Jan RR Verlet
Keyword(s):  
Structural Changes ◽  
Biological Response ◽  
Photoactive Yellow Protein

Photoactive proteins typically rely on structural changes in a small chromophore to initiate a biological response. While these changes often involve isomerization as the “primary step”, preceding this is an...

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