Zirak, Peyman and Penzkofer, Alfons and Lehmpfuhl, C. and Mathes, T. and Hegemann, P. (2007) Absorption and emission spectroscopic characterisation of blue-light receptor Slr1694 from Synechocystis sp. PCC6803. Journal of Photochemistry and Photobiology B: Biology 86 (1), pp. 22-34.
Download (633kB) - Repository staff only
Other URL: http://www.sciencedirect.com/science?_ob=ArticleURL&_udi=B6TH0-4KY88MJ-1&_user=616165&_coverDate=01%2F03%2F2007&_rdoc=4&_fmt=summary&_orig=browse&_srch=doc-info(%23toc%235268%232007%23999139998%23638888%23FLA%23display%23Volume)&_cdi=5268&_sort=d&_docanch
The BLUF protein Slr1694 from the cyanobacterium Synechocystis sp. PCC6803 is characterized by absorption and emission spectroscopy. Slr1694 expressed from E. coli which non-covalently binds FAD, FMN, and riboflavin (called Slr1694I), and reconstituted Slr1694 which dominantly contains FAD (called Slr1694II) are investigated. The receptor conformation of Slr1694 (dark adapted form Slr1694r) is ...
Export bibliographical data
|Institutions:||Physics > Institute of Experimental and Applied Physics > Alumni or Retired Professors > Group Alfons Penzkofer|
|Keywords:||BLUF domain; Slr1694 protein from Synechocystis sp. PCC6803; Blue-light photoreceptor; Absorption spectroscopy; Fluorescence spectroscopy; Photo-cycle; Photo-reduction; Flavoprotein; Flavins; FAD; FMN; Riboflavin|
|Dewey Decimal Classification:||500 Science > 530 Physics|
|Refereed:||Yes, this version has been refereed|
|Created at the University of Regensburg:||Yes|
|Deposited On:||20 Mar 2007|
|Last Modified:||13 Mar 2014 10:08|