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Trans-cis isomerization is responsible for the red-shifted fluorescence in variants of the red fluorescent protein eqFP611.
J Am Chem Soc 2008; 130(38):12578-9JA

Abstract

An important class of red fluorescent proteins (RFPs) feature a 2-iminomethyl-5-(4-hydroxybenzylidene)imidazolinone chromophore. Among these proteins, eqFP611 has the chromophore in a coplanar trans orientation, whereas the cis isomer is preferred by other RFPs such as DsRed and its variants. In the photoactivatable protein asFP595, the chromophore can even be switched from the nonfluorescent trans to the fluorescent cis state by light. By using X-ray crystallography, we have determined the structure of dimeric eqFP611 at high resolution (up to 1.1 A). In the far-red emitting eqFP611 variant d2RFP630, which carries an additional Asn143Ser mutation, the chromophore resides predominantly (approximately 80%) in the cis isomeric state, and in RFP639, which has Asn143Ser and Ser158Cys mutations, the chromophore is found completely in the cis form. The pronounced red shift of excitation and emission maxima of RFP639 can thus unambiguously be assigned to trans-cis isomerization of the chromophore. Among RFPs, eqFP611 is thus unique because its chromophore is highly fluorescent in both the cis and trans isomeric forms.

Authors+Show Affiliations

Institute of Biophysics, University of Ulm, Albert-Einstein-Allee 11, 89081 Ulm, Germany.No affiliation info availableNo 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

18761441

Citation

Nienhaus, Karin, et al. "Trans-cis Isomerization Is Responsible for the Red-shifted Fluorescence in Variants of the Red Fluorescent Protein EqFP611." Journal of the American Chemical Society, vol. 130, no. 38, 2008, pp. 12578-9.
Nienhaus K, Nar H, Heilker R, et al. Trans-cis isomerization is responsible for the red-shifted fluorescence in variants of the red fluorescent protein eqFP611. J Am Chem Soc. 2008;130(38):12578-9.
Nienhaus, K., Nar, H., Heilker, R., Wiedenmann, J., & Nienhaus, G. U. (2008). Trans-cis isomerization is responsible for the red-shifted fluorescence in variants of the red fluorescent protein eqFP611. Journal of the American Chemical Society, 130(38), pp. 12578-9. doi:10.1021/ja8046443.
Nienhaus K, et al. Trans-cis Isomerization Is Responsible for the Red-shifted Fluorescence in Variants of the Red Fluorescent Protein EqFP611. J Am Chem Soc. 2008 Sep 24;130(38):12578-9. PubMed PMID: 18761441.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Trans-cis isomerization is responsible for the red-shifted fluorescence in variants of the red fluorescent protein eqFP611. AU - Nienhaus,Karin, AU - Nar,Herbert, AU - Heilker,Ralf, AU - Wiedenmann,Jörg, AU - Nienhaus,G Ulrich, Y1 - 2008/08/30/ PY - 2008/9/3/pubmed PY - 2008/12/17/medline PY - 2008/9/3/entrez SP - 12578 EP - 9 JF - Journal of the American Chemical Society JO - J. Am. Chem. Soc. VL - 130 IS - 38 N2 - An important class of red fluorescent proteins (RFPs) feature a 2-iminomethyl-5-(4-hydroxybenzylidene)imidazolinone chromophore. Among these proteins, eqFP611 has the chromophore in a coplanar trans orientation, whereas the cis isomer is preferred by other RFPs such as DsRed and its variants. In the photoactivatable protein asFP595, the chromophore can even be switched from the nonfluorescent trans to the fluorescent cis state by light. By using X-ray crystallography, we have determined the structure of dimeric eqFP611 at high resolution (up to 1.1 A). In the far-red emitting eqFP611 variant d2RFP630, which carries an additional Asn143Ser mutation, the chromophore resides predominantly (approximately 80%) in the cis isomeric state, and in RFP639, which has Asn143Ser and Ser158Cys mutations, the chromophore is found completely in the cis form. The pronounced red shift of excitation and emission maxima of RFP639 can thus unambiguously be assigned to trans-cis isomerization of the chromophore. Among RFPs, eqFP611 is thus unique because its chromophore is highly fluorescent in both the cis and trans isomeric forms. SN - 1520-5126 UR - https://www.unboundmedicine.com/medline/citation/18761441/Trans_cis_isomerization_is_responsible_for_the_red_shifted_fluorescence_in_variants_of_the_red_fluorescent_protein_eqFP611_ L2 - https://dx.doi.org/10.1021/ja8046443 DB - PRIME DP - Unbound Medicine ER -