Near-Infrared Photoluminescence and Reversible Trans-to-Cis Photoisomerization of Mononuclear and Binuclear Ytterbium(III) Complexes Functionalized by Azobenzene Groups.

Two mononuclear and one binuclear ytterbium complexes with dual near-infrared (NIR) photoluminescence and reversible trans-to-cis photoisomerization functions were synthesized and characterized. The central ytterbium(III) ion coordinates with two β-diketonate (4,4,4-trifluoro-1-phenylbutane-1,3-dionate (tfd)) ligands and one deprotonated azobenzene-containing tetradentate ligand [()-4-(phenyldiazenyl)-,-bis(pyridin-2-ylmethyl) benzohydrazide (HL), ()-4-((4-(dimethylamino)phenyl)diazenyl)-,-bis(pyridin-2-ylmethyl)benzohydrazide (HNL), or ()-4,4'-','-bis(pyridin-2-ylmethyl)benzohydrazide azobenzene (HDL)] to form a neutral ternary complex ([Yb(tfd)L], [Yb(tfd)(NL)], or [Yb(tfd)(DL)], respectively), where the ytterbium(III) ion is eight-coordinated to NO donor sets. X-ray crystallographic analysis shows that all three complexes form a trigonal dodecahedron geometry with similar -N=N- distances that are slightly longer than those of the pure azobenzene-containing ligands.

Functionalized Lanthanide(III) Complexes Constructed from Azobenzene Derivative and β-Diketone Ligands: Luminescent, Magnetic, and Reversible Trans-to-Cis Photoisomerization Properties.

The coordination ability of ligands functionalized by azobenzene was manipulated, and two novel chelating ligands, (E)-4-(phenyldiazenyl)-N,N-bis(pyridin-2-ylmethyl) benzohydrazide (CHNO, PBPM) and (E)-4-((4-(dimethylamino)phenyl)diazenyl)-N,N-bis(pyridin-2-ylmethyl) benzohydrazide (CHNO, dmPBPM), were synthesized. The ligands can offer four coordinating atoms (one oxygen and three nitrogens) to act as tetradendate ligands, together with the two β-diketonates (4,4,4-trifluoro-1-phenylbutane-1,3-dionate, tfd), and the trifluoroacetate anion presented as a ligand and a counterion to form the quaternary units with lanthanide(III) ions (La, Eu, and Gd), [Ln(tfd)(PBPM)(CFCO)] (LnCHFNO) and [Ln(tfd)(dmPBPM)(CFCO)] (LnCHFNO), where the lanthanide(III) ions are nine coordinated with NO donor sets. All six complexes were structurally characterized, and four crystals were obtained and further analyzed by means of single-crystal X-ray diffraction.

Azobenzene-derived tris-β-diketonate lanthanide complexes: reversible trans-to-cis photoisomerization in solution and solid state.

Novel azobenzene-derived β-diketonates (4,4,5,5,6,6,6-heptafluoro-1-azobenzene-1,3-hexanedione (LA), 4,4,5,5,6,6,6-heptafluoro-1-(4-dimethylamino)azobenzene-1,3-hexanedione (LB)) were designed and their complexes with lanthanide cations (La(3+), Eu(3+), Gd(3+), Yb(3+)) were prepared and characterized by (1)H NMR, FT-IR, and elemental analysis. Three of the complexes were crystallized successfully and identified by X-ray diffraction. It was significant to find that LA showed remarkably reversible trans-to-cis isomerization properties, however, LB, bearing an electron donor compared with LA, slowed down the isomerization to an extent.

The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK.

The Raf-MEK-ERK pathway regulates many fundamental biological processes, and its activity is finely tuned at multiple levels. The Raf kinase inhibitory protein (RKIP) is a widely expressed negative modulator of the Raf-MEK-ERK signaling pathway. We have previously shown that RKIP inhibits the phosphorylation of MEK by Raf-1 through interfering with the formation of a kinase-substrate complex by direct binding to both Raf-1 and MEK.

Raf kinase inhibitor protein positively regulates cell-substratum adhesion while negatively regulating cell-cell adhesion.

Raf kinase inhibitor protein (RKIP) regulates a number of cellular processes, including cell migration. Exploring the role of RKIP in cell adhesion, we found that overexpression of RKIP in Madin-Darby canine kidney (MDCK) epithelial cells increases adhesion to the substratum, while decreasing adhesion of the cells to one another. The level of the adherens junction protein E-cadherin declines profoundly, and there is loss of normal localization of the tight junction protein ZO-1, while expression of the cell-substratum adhesion protein beta1 integrin dramatically increases.