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. 2009 Aug 5;131(30):10356-7.
doi: 10.1021/ja903695n.

Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima

Sebastien Violot  1 , Philippe Carpentier, Laurent Blanchoin, Dominique Bourgeois
Affiliations

Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima

Sebastien Violot et al. J Am Chem Soc. .

Abstract

The recently developed red fluorescent protein Keima exhibits the largest Stokes shift (180 nm) observed to date. Combining X-ray crystallography with (in crystallo) UV-visible absorption, fluorescence, and Raman spectroscopy, we have investigated molecular determinants of this peculiar property. The results demonstrate a pH-dependent "reverse chromophore protonation" triggered by the key residue Asp157 and which couples to cis/trans isomerization of the chromophore. These data provided guidelines to rationally design a useful Keima variant.

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