The interaction of lithium ions with two pyrimidine nucleobases, thymine and uracil, as well as the solvation of various complexes by one and two water molecules, has been studied in the gas phase. IRMPD spectra are reported for each of B-Li(+)-(H(2)O)(n) (n = 1-2) and B(2)-Li-(H(2)O)(m) (m = 0-1) for B = thymine, uracil over the 2500-4000 cm(-1) region. Calculations were performed using the B3LYP density functional in conjunction with the 6-31+G(d,p) basis set to model the vibrational spectra as well as MP2/6-311++G(2d,p) theory to model the thermochemistry of potential structures. Experimental and theoretical results were used in combination to determine structures of each complex, which are reported here. The lithium cation in all complexes was found to bond to the O4 oxygen in both thymine and uracil, and the first two water molecules of solvation were found to bond to Li(+). The experimental spectra obtained for BLi(+)(H(2)O)(n) (n = 1-2) and B(2)Li(+) for thymine and uracil clearly resemble one another, suggesting similar structural features in terms of bonding between the base and Li(+), as well as for solvation. This was confirmed through theoretical work. The addition of water to the lithium ion-bound DNA base dimers has been shown to induce a significant change in structure of the dimer to a hydrogen-bonded system similar to base pairing in the Watson-Crick model of DNA.
The proton- and the sodium ion-bound glycine homodimers are studied by a combination of infrared multiple photon dissociation (IRMPD) spectroscopy in the N-H and O-H stretching region and electronic structure calculations. For the proton-bound glycine dimer, in the region above 3100 cm (-1), the present spectrum agrees well with one recorded previously. The present work also reveals a weak, broad absorption spanning the region from 2650 to 3300 cm (-1). This feature is assigned to the strongly hydrogen-bonded and anharmonic N-H and O-H stretching modes. As well, the shared proton stretch is observed at 2440 cm (-1). The IRMPD spectra for the proton-bound glycine dimer confirms that the lowest energy structure is an ion-dipole complex between N-protonated glycine and the carboxyl group of the second glycine. This spectrum also helps to eliminate the existence of any of the higher-energy structures considered. The IRMPD spectrum for the sodium ion-bound dimer is a much simpler spectrum consisting of three bands assigned to the O-H stretch and the asymmetric and symmetric NH 2 stretching modes. The positions of these bands are very similar to those observed for the proton-bound glycine dimer. Numerous structures were considered and the experimental spectrum agrees with the B3LYP/6-31+G(d,p) predicted spectrum for the lowest energy structure, two bidentate glycine molecules bound to Na (+). Though some of the structures cannot be completely ruled out by comparing the experimental and theoretical spectra, they are energetically disfavored by at least 20 kJ mol (-1).
Structural aspects of proton-bound dimers composed of amino acids with aliphatic side chains are investigated using infrared multiple photon dissociation (IRMPD) spectroscopy and electronic structure calculations. Features in the IRMPD spectra in the 700-2,000 cm-1 range are due primarily to C=O stretching, NH2 bending, and COH bending. It was possible to distinguish between isomeric structures by comparing the experimental IRMPD spectra and those predicted using B3LYP/6-31+G(d,p). It was possible, based on the calculations and IRMPD spectra, to assign the experimental spectrum of the glycine proton-bound dimer to a structure which was slightly different from that assigned by previous spectroscopic investigations and in agreement with recent thermochemical studies. Since all proton-bound dimers studied here, composed of the different amino acids, have very similar spectra, it is expected that they also have very similar lowest-energy structures including the mixed alanine/glycine proton-bound dimer. In fact, the spectra are so similar that it would be very challenging to distinguish, for example, the glycine proton-bound dimer from the alanine or valine proton-bound dimers in the 700-2,000 cm-1 range. According to the calculated IR spectra it is shown that in the approximately 2,000-3,200 cm-1 range differentiating between different structures as well as different proton-bound dimers may be possible. This is due mainly to differences in the asymmetric stretch of the binding proton which is predicted to occur in this region.
Complexes between adenine and the alkali metal ions Li(+), Na(+), K(+), and Cs(+) have been investigated by infrared multiple photon dissociation (IRMPD) spectroscopy between 2800 and 3900 cm(-1), as have some singly hydrated complexes. The IRMPD spectra clearly show the N-H stretching and the NH(2) symmetric and asymmetric stretching vibrations of adenine; and for the solvated ions, the O-H stretching vibrations are observed. These experimental spectra were compared with those for a variety of possible structures, including both A9 (A9 refers to the tautomer where hydrogen is on the nitrogen in position 9 of adenine, see Scheme 1) and A7 adenine tautomers, computed using B3-LYP/6-31+G(d,p). By comparing the experimental and the simulated spectra it is possible to rule out various structures and to further assign structures to the species probed in these experiments. Single-point calculations on the B3-LYP/6-31+G(d,p) geometries have been performed at MP2/6-311++G(2d, p) to obtain good estimates of the relative thermochemistries for the different structures. In all cases the computed IR spectrum for the lowest energy structure is consistent with the experimental IRMPD spectrum, but in some cases structural assignment cannot be confirmed based solely upon comparison with the experimental spectra so computed thermochemistries can be used to rule out high-energy structures. On the basis of the IRMPD spectra and the energy calculations, all adenine-M(+) and adenine-M(+)-H(2)O are concluded to be composed of the A7 tautomer of adenine, which is bound to the cations in a bidentate fashion through N3 and N9 (see Scheme 1 for numbering convention). For the hydrated ions water binds directly to the metal ion through oxygen, as would be expected since the metal contains most positive charge density. For the hydrated lithium cation-bound adenine dimer, the water molecule is concluded to be hydrogen bonded to a free basic site of one of the adenine monomers, which is also bound to the lithium cation. Experimental and theoretical results on adenine-Li(+)-H(2)O suggest that the electrosprayed adenine-Li(+) resembles the lowest-energy solution phase ion rather than the lowest-energy gas-phase ion, which is the imine form.
With the development of soft ionization techniques such as electrospray ionization (ESI), mass spectrometry (MS) has found widespread application in structural biology. The ability to transfer large biomolecular complexes intact into the gas-phase, combined with the low sample consumption and high sensitivity of MS, has made ESI-MS a method of choice for the characterization of macromolecules. This paper describes the application of MS to study large non-covalent complexes. We categorize the available techniques in two groups. First, solution-based techniques in which the biomolecules are labeled in solution and subsequently characterized by MS. Three MS-based techniques are discussed, namely hydroxyl radical footprinting, cross-linking and hydrogen/deuterium exchange (HDX) MS. In the second group, MS-based techniques to probe intact biomolecules in the gas-phase, e.g. side-chain microsolvation, HDX and ion mobility spectrometry are discussed. Together, the approaches place MS as a powerful methodology for an ever growing plethora of structural applications.
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