Field-induced thermal metal-to-insulator transition in underdoped La(2-x)Sr(x)CuO(4+delta)

The transport of heat and charge in cuprates was measured in single crystals of La(2-x)Sr(x)CuO(4+delta) (LSCO) across the doping phase diagram at low temperatures. In underdoped LSCO, the thermal conductivity is found to decrease with increasing magnetic field in the T-->0 limit, in striking contrast to the increase observed in all superconductors, including cuprates at higher doping. In heavily underdoped LSCO, where superconductivity can be entirely suppressed with an applied magnetic field, we show that a novel thermal metal-to-insulator transition takes place upon going from the superconducting state to the field-induced normal state.     

Synthesis of 5,12-dioxocyclam nickel (II) complexes having quinoxaline substituents at the 6 and 13 positions as potential DNA bis-intercalating and cleaving agents

Several dioxocyclams containing quinoxaline moieties, as well as their nickel(II) complexes were synthesized and studied for their ability to bind and oxidatively cleave DNA. Although no evidence for binding by intercalation was found, the ability of the Ni(II) complexes to cleave DNA in the presence of Oxone was strongly dependent on both the nature and the spatial orientation of the quinoxaline moieties, suggesting at least transient association of these complexes with DNA.     

Neutral and dianionic iron and ruthenium 1,4-diphosphabutadiene complexes

Reaction of a tetraphenyl-1,2-diphosphinyl dianion with [FeCl2(THF)1.5] or [Ru(COD)(acac)2] yields dianionic complexes which further react with Ph3SnCl to afford the corresponding bis(1,4-diphosphabutadiene) complexes.     

Structure and mechanism of action of isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase

We have obtained the three-dimensional X-ray crystallographic structure of a C67A mutant Escherichia coli isopentenylpyrophosphate-dimethylallylpyrophosphate isomerase (EC 5.3.3.2) complexed with the bromohydrin of isopentenylpyrophosphate, at 1.93 A resolution. The overall backbone fold is very similar to that obtained previously for the wild-type enzyme in the presence of a divalent metal cation (Mn2+ or Mg2+). However, in the new structure, there are two metal binding sites, not just one. The first metal binding site is occupied by Mn2+, coordinated to three histidine and two glutamate residues, while the second is occupied by Mg2+, coordinated to two bromohydrin-ligand phosphate oxygens, the carbonyl oxygen of A67, a carboxyl oxygen of E87, and two water molecules. The C3 hydroxyl group of the bromohydrin inhibitor is involved in a short hydrogen bond to the carboxyl group of E116, one of the two Mn-bound glutamates. The structure obtained is consistent with a mechanism of action of the enzyme in which the carboxyl group of E116 protonates the double bond in isopentenylpyrophosphate, forming a carbocation, followed by removal of a C2 proton by the thiolate of C67, in the wild-type enzyme. The inhibition of the enzyme by a wide variety of other potent inhibitors is also readily explained on the basis of the bromohydrin inhibitor structure.     

A fluorogenic dye activated by the staudinger ligation

Specific labeling of biomolecules with biochemical and biophysical probes is a central element of proteomics research. Here we describe a coumarin-phosphine dye that undergoes activation of coumarin fluorescence upon Staudinger ligation with azides. Since azides can be metabolically incorporated into cellular proteins and oligosaccharides, this dye may be a useful tool for profiling proteins and their posttranslational modifications.     

A planar tetracoordinate carbon and unusual bonding in an organodimetallic propynylidene complex arising from double C-H activation of an allene ligand

Reduction of the organoditantalum allene complex (eta-C5Me4R)2Ta2(mu-X)X3(mu-eta1,eta3-C3H4) (R = Me (Cp*), Et; X = Cl, Br) with sodium amalgam leads to the propynylidene complex (eta-C5Me4R)2Ta2(mu-H)2X2(mu-HCCCH) by a formal double 1,3-C-H activation of the allene ligand. The solid-state molecular structure contains a planar HCCCH ligand bridging, in parallel coordination mode, the two tantalum atoms, with the HCCCH and Ta atoms coplanar. Key structural features are a Ta-Ta distance of 2.8817(7) A, propynylidene C-C-C angle of 153.7(13) degrees , C-C distance of 1.370(8) A, Ta-C(central) distance of 2.194(9) A, and Ta-C(terminal) distance of 1.970(9) A. Molecular orbital calculations on the complex at the RHF/SBK(d) and B3LYP/LanL2dz levels of theory demonstrate that the propynylidene ligand is best viewed formally as an allenediylidene(4-) ligand bonded to two d0 tantalum atoms via two Ta=C(terminal) double bonds and an unusual three-center, two-electron bridge bond involving both tantalum atoms and a lone pair on the planar, tetracoordinate central carbon. There is no net Ta-Ta bonding based on the orbital analysis.     

Characterization of the cholesteric phase of filamentous bacteriophage fd for molecular alignment

Residual dipolar couplings arise from small degrees of alignment of molecules in a magnetic field and have proven to provide valuable structural information. Colloidal suspensions of rod-shaped viruses and bacteriophages constitute a frequently employed medium for imparting such alignment onto biomolecules. The stability and behavior of the liquid crystalline phases with respect to solution conditions such as pH, ionic strength, and temperature vary, and characterization should benefit practical applications as well as theoretical understanding. In this Communication we describe the pH dependence of the cholesteric liquid crystalline phase of the filamentous bacteriophage fd and demonstrate that the alignment tensor of the solute protein is modulated by pH. We also report the interesting observation that the relative sign of the residual dipolar coupling changes at low pH values. In addition, we demonstrate that the degree of alignment inversely scales with the lengths of the phage particles for phages with identical mass and charge per unit length.