Skip Navigation



Plant and Cell Physiology Advance Access published online on January 19, 2005

Plant and Cell Physiology, doi:10.1093/pcp/pci003
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
46/1/136    most recent
pci003v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Hasegawa, K.
Right arrow Articles by Ono, T.-a.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hasegawa, K.
Right arrow Articles by Ono, T.-a.
Agricola
Right arrow Articles by Hasegawa, K.
Right arrow Articles by Ono, T.-a.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights researved.
Received September 10, 2004
Accepted October 23, 2004

Regular Paper

Spectroscopic Analysis of the Dark Relaxation Process of a Photocycle in a Sensor of Blue-Light Using FAD (BLUF) Protein Slr1694 of Cyanobacterium Synechocystis sp. PCC6803

Koji Hasegawa 1, Shinji Masuda 1, and Taka-aki Ono 1*

1 Laboratory for Photo-Biology (I), RIKEN Photodynamics Research Center, The Institute of Physical and Chemical Research, 519-1399 Aoba, Aramaki, Aoba, Sendai 980-0845, Japan

* To whom correspondence should be addressed.
Taka-aki Ono, E-mail: takaaki{at} riken.jp


   Abstract

Slr1694 is a BLUF (sensor of blue-light using flavin adenine dinucleotide) protein and a putative photoreceptor in the cyanobacterium Synechocystis sp. PCC 6803. Illumination of Slr1694 induced a signaling light-state concurrent with a red-shift in the UV-visible absorption of flavin, and formation of the bands from flavin and apo-protein in the light-minus-dark Fourier-transform infrared (FTIR) difference spectrum. Replacement of tyrosine 8 with phenylalanine abolished these changes. The light-state relaxed to the ground dark state, during which the FTIR bands decayed monophasically. These bands were classifiable into three groups according to their decay rates. The C4=O stretching bands of a flavin isoalloxazine ring had the highest decay rate, which corresponded to that of the absorption red-shift. The result indicated that the hydrogen bonding at C4=O is responsible for the UV-visible red-shift, in consistent with the results of density functional calculation. All FTIR bands and the red-shift decayed at the same slower rate in deuterated Slr1694. These results indicated that the dark relaxation from the light-state is limited by the proton transfer. In contrast, a constrained light-state formed under dehydrated conditions decayed much slower with no deuteration effects. A photocycle mechanism involving the proton transfer was proposed.

Keywords: photoreceptor; flavin; FTIR; signal transduction; blue light; isoalloxazine ring.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
Plant Cell PhysiolHome page
S. Masuda, K. Hasegawa, H. Ohta, and T.-a. Ono
Crucial Role in Light Signal Transduction for the Conserved Met93 of the BLUF Protein PixD/Slr1694
Plant Cell Physiol., October 1, 2008; 49(10): 1600 - 1606.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
M. Gauden, I. H. M. van Stokkum, J. M. Key, D. Ch. Luhrs, R. van Grondelle, P. Hegemann, and J. T. M. Kennis
Hydrogen-bond switching through a radical pair mechanism in a flavin-binding photoreceptor
PNAS, July 18, 2006; 103(29): 10895 - 10900.
[Abstract] [Full Text] [PDF]


Home page
Plant Cell PhysiolHome page
S. Masuda, K. Hasegawa, and T.-a. Ono
Tryptophan at Position 104 is Involved in Transforming Light Signal into Changes of {beta}-sheet Structure for the Signaling State in the BLUF Domain of AppA
Plant Cell Physiol., December 1, 2005; 46(12): 1894 - 1901.
[Abstract] [Full Text] [PDF]


Home page
Proc. Natl. Acad. Sci. USAHome page
A. Jung, T. Domratcheva, M. Tarutina, Q. Wu, W.-h. Ko, R. L. Shoeman, M. Gomelsky, K. H. Gardner, and I. Schlichting
Structure of a bacterial BLUF photoreceptor: Insights into blue light-mediated signal transduction
PNAS, August 30, 2005; 102(35): 12350 - 12355.
[Abstract] [Full Text] [PDF]


Home page
J BiochemHome page
K. Okajima, S. Yoshihara, Y. Fukushima, X. Geng, M. Katayama, S. Higashi, M. Watanabe, S. Sato, S. Tabata, Y. Shibata, et al.
Biochemical and Functional Characterization of BLUF-Type Flavin-Binding Proteins of Two Species of Cyanobacteria
J. Biochem., June 1, 2005; 137(6): 741 - 750.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.