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- DOI to cite this document:
- 10.5283/epub.1899
Abstract
The BLUF protein Slrl694 from the cyanobacterium Synechocystis sp. PCC6803 is characterized by absorption and emission spectroscopy. Slrl694 expressed from E. coli which non-covalently binds FAD, FMN, and riboflavin (called Slr1694(I)), and reconstituted Sh-1694 which dominantly contains FAD (called Slr1694(II)) are investigated. The receptor conformation of Slrl694 (dark adapted form Slr1694(r)) ...

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