Phenyl substitution of cationic bis-cyclometalated iridium(iii) complexes for iTMC-LEECs.

A series of seven cationic bis-cyclometalated iridium(iii) complexes of the form [(C^N)2(N^N)Ir][PF6] has been designed in order to examine the effect of bulky, hydrophobic phenyl substituents on the structure-property relationship of these ionic transition metal complexes (iTMCs) in light-emitting electrochemical cells (LEECs). Capping phenyl substituents on the cyclometalating and ancillary ligands allows for individual tuning of the HOMO and LUMO energy levels, respectively, yielding an emission range from yellow to red. The complexes in this series exhibit increased quantum yields, up to 70% higher than the unoptimized, archetypal [(2-phenylpyridine)2(2,2'-bipyridine)Ir][PF6]. Among these, one complex, C3, was recently reported to produce devices with superior luminance and efficiency. Simultaneous measure of the series of complexes enabled the clear discernment of trends in device performance connected to fundamental structure-property relationships that elucidate the origin of enhanced luminance. In general, phenyl substitution of the 2-phenylpyridine ligands of the parent complex produced higher luminance and faster device response than phenyl substitution of the 2,2'-bipyridine ligand. Overall, complex design and device engineering produce competitive LEECs from simple, single-layer architectures. The synthesis, crystallographic, photophysical, and electrochemical properties of the iTMCs, along with the electroluminescence properties of the LEEC devices are reported herein.

Massive palmitoylation-dependent endocytosis during reoxygenation of anoxic cardiac muscle.

In fibroblasts, large Ca transients activate massive endocytosis (MEND) that involves membrane protein palmitoylation subsequent to mitochondrial permeability transition pore (PTP) openings. Here, we characterize this pathway in cardiac muscle. Myocytes with increased expression of the acyl transferase, DHHC5, have decreased Na/K pump activity. In DHHC5-deficient myocytes, Na/K pump activity and surface area/volume ratios are increased, the palmitoylated regulatory protein, phospholemman (PLM), and the cardiac Na/Ca exchanger (NCX1) show greater surface membrane localization, and MEND is inhibited in four protocols. Both electrical and optical methods demonstrate that PTP-dependent MEND occurs during reoxygenation of anoxic hearts. Post-anoxia MEND is ablated in DHHC5-deficient hearts, inhibited by cyclosporine A (CsA) and adenosine, promoted by staurosporine (STS), reduced in hearts lacking PLM, and correlates with impaired post-anoxia contractile function. Thus, the MEND pathway appears to be deleterious in severe oxidative stress but may constitutively contribute to cardiac sarcolemma turnover in dependence on metabolic stress. DOI: http://dx.doi.org/10.7554/eLife.01295.001.

Toward an understanding of the complete NCX1 lifetime in the cardiac sarcolemma.

The density of Na/Ca exchangers (NCX1) in the cardiac sarcolemma, like all plasma membrane proteins, will be influenced by (and ultimately determined by) the function of membrane insertion and retrieval processes (i.e., exo- and endocytic mechanisms). Progress in understanding these processes in cardiac muscle faces many biological and methodological complexities and hurdles. As described here, we are attempting to overcome these hurdles to study more adequately the assembly and disassembly of the cardiac sarcolemma, in general, and the control of NCX1 by membrane trafficking processes in particular. First, we have developed improved noninvasive methods to monitor the cellular capacitance of cardiac tissue (NIC) over periods of hours. Thus, we can study long-term changes of total membrane area. Second, we have developed mice that express fusion proteins of NCX1 with the pHluorin green protein. Thus, we can determine the membrane disposition of NCX1, and changes thereof, on-line in intact cardiac muscle.