The observation of incomplete on/off switching of rsGreen1 at different pH as well as a different initial first cycle can be quantitatively described by our simple 4-state model presented in this work.

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Reversibly switchable monomeric Cherry (rsCherry) is a photoswitchable variant of the red fluorescent protein mCherry. We report that this protein gradually and irreversibly loses its red fluorescence in the dark over a period of months at 4°C and a few days at 37°C. We also find that its ancestor, mCherry, undergoes a similar fluorescence loss but at a slower rate. X-ray crystallography and mass spectrometry reveal that this is caused by the cleavage of thep-hydroxyphenyl ring from the chromophore and the formation of two novel types of cyclic structures at the remaining chromophore moiety. Overall, our work sheds light on a new process occurring within fluorescent proteins, further adding to the chemical diversity and versatility of these molecules.

In the title organoplatinum(II) complex, [PtCl2(C5H5N)(C11H14O2)], the methyleugenol ligand only coordinates to the PtIIatom through the ethylenic double bond. The coordination is completed by the N atom of the pyridine ligand and two Cl atoms positionedtranswith respect to each other. The pyridine and benzene rings are inclined to one another by 68.6 (2)°. In the crystal, molecules are linkedviaa number of C—H...Cl and C—H...O hydrogen bonds, forming sheets parallel to thebcplane.