01831nas a2200181   4500008004100000245010100041210006900142260000800211300001600219490000600235520117900241100002401420700002101444700001901465700001901484700002101503856012501524       2011                        eng d00aCorrection to what drives the redox properties of model green fluorescence protein chromophores?0 aCorrection to what drives the redox properties of model green fl  cOCT  a2695–26950 v23 a<p>We report the first experimental determination of the oxidation potentials E-ox(0). (relative to the standard hydrogen electrode, SHE) of model green fluorescent protein (GFP) chromophores. Para-, meta, and ortho-hydroxy (4-hydroxybenzylidene-2,3-dimethylimidazolinone, HBDI) and methoxy (MeOBDI) derivatives were studied. E-ox(0) of the three isomers in acetonitrile are -1.31, -1.52, and -1.39 V, respectively. Electronic structure calculations reproduce the observed differences between the isomers and reveal that E-ox(0) follows the ionization energies (IEs), that is, p-MeOBDI has the lowest IE (6.96 eV in the gas phase) due to resonance stabilization of its cation, whereas the resonance is detuned in m-MeOBDL resulting in more-negative E-ox(0). The observed meta and ortho effects in E-ox(0) are similar to the trends in pK(a). The effect of increased solvent polarity on absolute.E-ox(0) (and especially on para-meta-ortho differences) was found to be small. The redox properties of GFP chromophores are driven by their structure and can be correlated with IEs, which can be exploited in predicting the properties of other fluorescent protein chromophores.</p>1 aSolntsev, Kyril, M.1 aGhosh, Debashree1 aAmador, Adrian1 aJosowicz, Mira1 aKrylov, Anna, I.  uhttps://library.ncl.res.in/content/correction-what-drives-redox-properties-model-green-fluorescence-protein-chromophores01771nas a2200169   4500008004100000245008700041210006900128260000800197490000600205520117200211100002401383700002101407700001901428700001901447700002101466856011401487       2011                        eng d00aWhat drives the redox properties of model green fluorescence protein chromophores?0 aWhat drives the redox properties of model green fluorescence pro  cSEP0 v23 aWe report the first experimental determination of the oxidation potentials E-ox(0). (relative to the standard hydrogen electrode, SHE) of model green fluorescent protein (GFP) chromophores. Para-, meta, and ortho-hydroxy (4-hydroxybenzylidene-2,3-dimethylimidazolinone, HBDI) and methoxy (MeOBDI) derivatives were studied. E-ox(0) of the three isomers in acetonitrile are -1.31, -1.52, and -1.39 V, respectively. Electronic structure calculations reproduce the observed differences between the isomers and reveal that E-ox(0) follows the ionization energies (IEs), that is, p-MeOBDI has the lowest IE (6.96 eV in the gas phase) due to resonance stabilization of its cation, whereas the resonance is detuned in m-MeOBDL resulting in more-negative E-ox(0). The observed meta and ortho effects in E-ox(0) are similar to the trends in pK(a). The effect of increased solvent polarity on absolute.E-ox(0) (and especially on para-meta-ortho differences) was found to be small. The redox properties of GFP chromophores are driven by their structure and can be correlated with IEs, which can be exploited in predicting the properties of other fluorescent protein chromophores.1 aSolntsev, Kyril, M.1 aGhosh, Debashree1 aAmador, Adrian1 aJosowicz, Mira1 aKrylov, Anna, I.  uhttps://library.ncl.res.in/content/what-drives-redox-properties-model-green-fluorescence-protein-chromophores