High Valent Mercury Fluoride Ions.

Mercury fluoride ions formed during the laser ablation of HgF2(s) show the formation of six different cluster ion series viz., HgFn ± , Hgn Fn-2 ± , Hgn Fn-1 ± , (HgF)n ± , Hgn Fn+1 ± , and Hgn Fn+2 ± . Among the different ion series, the observation of high valent HgFn ± (n ± =3,4; n - =6-8) indicates the existence of corresponding molecules which signify the remarkable participation of 5d Hg electrons in the chemical bonding with F atoms and thus make Hg a truly transition metal. Further, molecular orbital calculations show a large HOMO-LUMO energy gap (≥3 eV) and high electron affinity (≥5 eV) that indicates highly stable HgFn=3,4,6,8 with super halogen properties.

Binding of Cu+ and Cu2+ with peptides: Peptides = oxytocin, Arg8 -vasopressin, bradykinin, angiotensin-I, substance-P, somatostatin, and neurotensin.

The intrinsic binding ability of 7 natural peptides (oxytocin, arg8 -vasopressin, bradykinin, angiotensin-I, substance-P, somatostatin, and neurotensin) with copper in 2 different oxidation states (CuI/II ) derived from different Cu+/2+ precursor sources have been investigated for their charge-dependent binding characteristics. The peptide-CuI/II complexes, [M - (n-1)H + nCuI ] and [M - (2n-1)H + nCuII ], are prepared/generated by the reaction of peptides with CuI solution/Cu-target and CuSO4 solution and are analyzed by using matrix-assisted laser desorption/ionization (MALDI) time-of-flight mass spectrometry. The MALDI mass spectra of both [M - (n-1)H + nCuI ] and [M - (2n-1)H + nCuII ] complexes show no mass shift due to the loss of ─H atoms in the main chain ─NH of these peptides by Cu+ and Cu2+ deprotonation. The measured m/z value indicates the reduction of CuI/II oxidation state into Cu0 during MALDI processes. The number and relative abundance of Cu+ bound to the peptides are greater compared with the Cu2+ bound peptides. Oxytocin, arg8 -vasopressin, bradykinin, substance-P, and somatostatin show the binding of 5Cu+ , and angiotensin-I and neurotensin show the binding of 7Cu+ from both CuI and Cu targets, while bradykinin shows the binding of 2Cu2+ , oxytocin, arg8 -vasopressin, angiotensin-I, and substance-P; somatostatin shows the binding of 3Cu2+ ; and neurotensin shows 4Cu2+ binding. The binding of more Cu+ with these small peptides signifies that the bonding characteristics of both Cu+ and Cu2+ are different. The amino acid residues responsible for the binding of both Cu+ and Cu2+ in these peptides have been identified based on the density functional theory computed binding energy values of Cu+ and the fragment transformation method predicted binding preference of Cu2+ for individual amino acids.

Theoretical prediction of rare gas containing hydride cations: HRgBF+ (Rg = He, Ar, Kr, and Xe).

The existence of rare-gas-containing hydride ions of boron (HRgBF(+)) has been predicted by using ab initio quantum chemical methods. The HRgBF(+) ions are obtained by inserting a rare gas (Rg) atom in between the H and B atoms of a HBF(+) ion, and the geometries are optimized for minima as well as transition states using second-order Møller-Plesset perturbation theory (MP2), density functional theory (DFT), and coupled-cluster theory (CCSD(T)) based techniques. The predicted HRgBF(+) ions are found to be metastable, and they exhibit a linear structure at the minima and a nonlinear planar structure at the transition state, corresponding to C∞v and Cs symmetries, respectively. All of the predicted HRgBF(+) ions show negative binding energies with respect to the two-body dissociation channel, leading to global minima (HBF(+) + Rg) on the singlet potential energy surface. In contrast, the dissociation energies corresponding to another two-body dissociation channel leading to HRg(+) + BF and two three-body dissociation channels corresponding to the dissociation into H + Rg + BF(+) and H(+) + Rg + BF show very high positive energies. Apart from positive dissociation energies, the predicted ions show finite barrier heights corresponding to the transition states involving a H-Rg-B bending mode, leading to the global minima products (HBF(+) + Rg). The finite barrier heights in turn would prevent the metastable HRgBF(+) species from transforming to global minima products. Structure, harmonic vibrational frequencies, stability, and Mulliken and natural bonding orbital (NBO) charge distribution values for all of the species are reported using the MP2 and DFT methods. Furthermore, the intrinsic reaction coordinate analysis confirms that the metastable minimum-energy structure and the global minimum products are connected through the corresponding transition state for each of the species on the respective singlet potential energy surface. Atoms-in-molecules (AIM) analysis indicates that the HRgBF(+) ions are best described as HRg(+)BF and are analogous to the isoelectronic HRgCO(+) and HRgN2(+) ions. The energetic along with charge redistribution and spectroscopic data strongly support the possible existence of HRgBF(+) ions. Hence, it might be possible to generate HRgBF(+) ions in the DC discharge plasma of a BF3/H2/Rg mixture at low temperature, and the predicted ions may be characterized using the magnetic field modulated infrared laser spectroscopic technique, which has been used earlier to characterize HBF(+) ions.

Characteristics and relaxation dynamics of van der Waals complexes between p-difluorobenzene and Ne.

Characteristics of the single and double Ne van der Waals complexes of p-difluorobenzene (pDFB) have been explored with ultraviolet fluorescence excitation and dispersed fluorescence spectroscopy. Eight S(1)-S(0) fluorescence excitation bands involving six ring modes of pDFB-Ne and two bands of pDFB-Ne(2) have been identified. Band assignments are confirmed by dispersed fluorescence from the pumped band. Shifts of the complex bands from the analogous monomer bands are generally 4 cm(-1) to the red for pDFB-Ne and 8 cm(-1) for pDFB-Ne(2). None of the observed ring modes is significantly perturbed by complexation in either the S(1) or S(0) states. The pDFB-Ne S(1) van der Waals binding energy D(0')