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Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima.
J Am Chem Soc 2009; 131(30):10356-7JA

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.

Authors+Show Affiliations

Institut de Recherches en Technologies et Sciences pour le Vivant, Laboratoire de Physiologie Cellulaire Végétale, CEA, CNRS, INRA, Université Joseph Fourier, 17 rue des Martyrs, F-38054 Grenoble, France.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19722611

Citation

Violot, Sebastien, et al. "Reverse pH-dependence of Chromophore Protonation Explains the Large Stokes Shift of the Red Fluorescent Protein MKeima." Journal of the American Chemical Society, vol. 131, no. 30, 2009, pp. 10356-7.
Violot S, Carpentier P, Blanchoin L, et al. Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima. J Am Chem Soc. 2009;131(30):10356-7.
Violot, S., Carpentier, P., Blanchoin, L., & Bourgeois, D. (2009). Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima. Journal of the American Chemical Society, 131(30), pp. 10356-7. doi:10.1021/ja903695n.
Violot S, et al. Reverse pH-dependence of Chromophore Protonation Explains the Large Stokes Shift of the Red Fluorescent Protein MKeima. J Am Chem Soc. 2009 Aug 5;131(30):10356-7. PubMed PMID: 19722611.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Reverse pH-dependence of chromophore protonation explains the large Stokes shift of the red fluorescent protein mKeima. AU - Violot,Sebastien, AU - Carpentier,Philippe, AU - Blanchoin,Laurent, AU - Bourgeois,Dominique, PY - 2009/9/3/entrez PY - 2009/9/3/pubmed PY - 2009/12/16/medline SP - 10356 EP - 7 JF - Journal of the American Chemical Society JO - J. Am. Chem. Soc. VL - 131 IS - 30 N2 - 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. SN - 1520-5126 UR - https://www.unboundmedicine.com/medline/citation/19722611/Reverse_pH_dependence_of_chromophore_protonation_explains_the_large_Stokes_shift_of_the_red_fluorescent_protein_mKeima_ L2 - https://dx.doi.org/10.1021/ja903695n DB - PRIME DP - Unbound Medicine ER -