Kinetics of and intermediates in a photocycle branching reaction of the photoactive yellow protein from Ectothiorhodospira halophila

FEBS Letters ◽  
1999 ◽  
Vol 458 (2) ◽  
pp. 252-256 ◽  
Author(s):  
Johnny Hendriks ◽  
Ivo H.M. van Stokkum ◽  
Wim Crielaard ◽  
Klaas J. Hellingwerf
Keyword(s):  
Photoactive Yellow Protein ◽  
Ectothiorhodospira Halophila ◽  
Kinetics Of

scholarly journals Femtosecond Spectroscopic Observations of Initial Intermediates in the Photocycle of the Photoactive Yellow Protein from Ectothiorhodospira halophila

1999 ◽  
Vol 77 (2) ◽  
pp. 1017-1023 ◽  
Author(s):  
Savitha Devanathan ◽  
Andrew Pacheco ◽  
Laszlo Ujj ◽  
Michael Cusanovich ◽  
Gordon Tollin ◽  
...  
Keyword(s):  
Photoactive Yellow Protein ◽  
Spectroscopic Observations ◽  
Ectothiorhodospira Halophila

Kinetics of the E46Q mutant of photoactive yellow protein investigated by transient grating spectroscopy

2017 ◽  
Vol 683 ◽  
pp. 262-267 ◽  
Author(s):  
Cheolhee Yang ◽  
Tae Wu Kim ◽  
Youngmin Kim ◽  
Jungkweon Choi ◽  
Sang Jin Lee ◽  
...  
Keyword(s):  
Photoactive Yellow Protein ◽  
Transient Grating ◽  
Transient Grating Spectroscopy ◽  
Grating Spectroscopy ◽  
Kinetics Of

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.

Active Site Mutants Implicate Key Residues for Control of Color and Light Cycle Kinetics of Photoactive Yellow Protein†

Biochemistry ◽  
1997 ◽  
Vol 36 (1) ◽  
pp. 8-14 ◽  
Author(s):  
Ulrich K. Genick ◽  
Savitha Devanathan ◽  
Terry E. Meyer ◽  
Ilona L. Canestrelli ◽  
Erica Williams ◽  
...  
Keyword(s):  
Active Site ◽  
Photoactive Yellow Protein ◽  
Light Cycle ◽  
Key Residues ◽  
Active Site Mutants ◽  
Kinetics Of ◽  
Color And Light

Kinetics of Proton Uptake and Dye Binding by Photoactive Yellow Protein in Wild Type and in the E46Q and E46A Mutants†

Biochemistry ◽  
2002 ◽  
Vol 41 (31) ◽  
pp. 10026-10037 ◽  
Author(s):  
Berthold Borucki ◽  
Savitha Devanathan ◽  
Harald Otto ◽  
Michael A. Cusanovich ◽  
Gordon Tollin ◽  
...  
Keyword(s):  
Photoactive Yellow Protein ◽  
Wild Type ◽  
Dye Binding ◽  
Proton Uptake ◽  
Kinetics Of
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