Article
Mutational analysis of Deinococcus radiodurans bacteriophytochrome reveals key amino acids necessary for the photochromicity and proton exchange cycle of phytochromes.
The Journal of biological chemistry - 2 May 2008
Wagner Jeremiah R, Zhang Junrui, von Stetten David, Günther Mina, Murgida Daniel H, Mroginski Maria Andrea, Walker Joseph M, Forest Katrina T, Hildebrandt Peter, Vierstra Richard D
Abstract excerpt
The ability of phytochromes (Phy) to act as photointerconvertible light switches in plants and microorganisms depends on key interactions between the bilin chromophore and the apoprotein that promote bilin attachment and photointerconversion between the spectrally distinct red light-absorbing Pr conformer and far red light-absorbing Pfr conformer. Using structurally guided site-directed mutagenesis combined with...
Topics
- Amino Acid Substitution
- Amino Acids
- Biliverdine
- Binding Sites
- Conserved Sequence
- DNA Mutational Analysis
- Deinococcus
- Fluorescence
- Hydrophobic and Hydrophilic Interactions