Charge-transfer luminescence from ruthenium(II) complexes containing tridentate ligands

Four complexes of the general formula Ru(NNN)²⁺₂ (N NN = tridentate N-heterocyclic ligand) were synthesized and studied spectroscopically. All exhibit visible absorption spectra that are charge-transfer-to-ligand in origin, are luminescent in glasses at 77 K, and display emission spectra that possess energies, structures, and decay tines that label them as charge transfer.     

The structural role of the carrier protein - active controller or passive carrier

Covering: 2007 to 2011. Previous review: Nat. Prod. Rep., 2007, 24, 750Common to all FASs, PKSs and NRPSs is a remarkable component, the acyl or peptidyl carrier protein (A/PCP). These take the form of small individual proteins in type II systems or discrete folded domains in the multi-domain type I systems and are characterized by a fold consisting of three major α-helices and between 60-100 amino acids. This protein is central to these biosynthetic systems and it must bind and transport a wide variety of functionalized ligands as well as mediate numerous protein-protein interactions, all of which contribute to efficient enzyme turnover. This review covers the structural and biochemical characterization of carrier proteins, as well as assessing their interactions with different ligands, and other synthase components. Finally, their role as an emerging tool in biotechnology is discussed.