2015
DOI: 10.5935/0103-5053.20150268
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Rhenium(I) Polypyridine Complexes as Luminescence-Based Sensors for the BSA Protein

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Cited by 3 publications
(2 citation statements)
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“…25,32,33,40 The emission maxima ranged from 600 to 635 nm, as shown in Figure S18, and are bathochromically shifted for Re-pyr, Re-ind, and Re-cbz in comparison to Re-phen as a result of a more efficient stabilization of the 3 MLCT Re→NN excited state by the presence of additional aromatic rings. 28,41,42 The PL quantum yields (Φ PL ) and lifetimes (τ PL ) increased in the order Re-cbz < Reind < Re-pyr < Re-phen, as shown in Table 2, following the decrease in the number of aromatic rings of the substituent in the NN ligand. The presence of the N-heterocyclic substituents favored the nonradiative decay that competes with the radiative deactivation of the excited state.…”
Section: Spectroscopic Electrochemical and Photophysicalmentioning
confidence: 99%
“…25,32,33,40 The emission maxima ranged from 600 to 635 nm, as shown in Figure S18, and are bathochromically shifted for Re-pyr, Re-ind, and Re-cbz in comparison to Re-phen as a result of a more efficient stabilization of the 3 MLCT Re→NN excited state by the presence of additional aromatic rings. 28,41,42 The PL quantum yields (Φ PL ) and lifetimes (τ PL ) increased in the order Re-cbz < Reind < Re-pyr < Re-phen, as shown in Table 2, following the decrease in the number of aromatic rings of the substituent in the NN ligand. The presence of the N-heterocyclic substituents favored the nonradiative decay that competes with the radiative deactivation of the excited state.…”
Section: Spectroscopic Electrochemical and Photophysicalmentioning
confidence: 99%
“…The association and/or interaction of Re(I) compound with the amino acid residues of the polypeptide chain of BSA induced a conformational change of the secondary structure of the protein with a decrease of its -helicity [90].…”
Section: Interactions Of Re-complexes With Proteinsmentioning
confidence: 99%