Absorption and emission spectroscopic characterisation of blue-light receptor Slr1694 from Synechocystis sp. PCC6803

DOI to cite this document:: 10.5283/epub.1899

Zirak, Peyman ; Penzkofer, Alfons ; Lehmpfuhl, C. ; Mathes, T. ; Hegemann, P.

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Date of publication of this fulltext: 05 Aug 2009 13:34

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Abstract

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 ...