Direct spectroscopic detection of a zwitterionic excited state.

Two electrons in two weakly coupled orbitals give rise to two states (diradical) with electrons residing in separate orbitals and two states (zwitterionic) with both electrons paired in one orbital or the other. This two-electron, two-orbital state manifold has eluded experimental confirmation because the zwitterionic states have been difficult to locate. Two-photon excitation of fluorescence from Mo(2)CI(4)(PMe(3))(4) (D2d) has been measured with linearly and circularly polarized light. From the polarization ratio and the energy of the observed transition, the 2(1)A(1) (delta*delta*) excited state has been located and characterized. In conjunction with the one-photon allowed (1)B(2) (deltadelta*) excited state, the zwitterionic state manifold for the quadruply bonded metal-metal class of compounds is thus established.

Understanding ion deceleration lenses: What are the simplicity/performance trade-offs?

The traditional approach for obtaining highly collimated low energy (<200 eV) beams from high-energy (1-10 keV) sector mass spectrometers involves the use of a complex exponential deceleration lens assembly. Through ion optical modeling of the exponential lens and other less-complex lens designs, the fundamental features that contribute to deceleration lens performance are investigated. From this evaluation, a simple high-performance lens was designed, constructed, and characterized. The novel lens described here decelerates a 3-keV ion beam down to the 3-200-eV range while providing low angular divergence, excellent focusing, and good transmission.

Chromophore interactions in flavocytochrome c552: a resonance Raman investigation.

Resonance Raman spectra with both Soret and visible excitation have been obtained for Chromatium flavocytochrome c552 and its isolated diheme subunit under varying conditions of pH and inhibitor binding. The spectra are generally consistent with previously established classification schemes for porphyrin ring vibrations. The presence of covalently bound flavin in the protein was apparent in the fluorescent background it produced and in flavin-mediated photoeffects observed in heme Raman spectra obtained at high laser power. No flavin modes were present in the Raman spectra, nor was any evidence of direct heme-flavin interaction found by using this technique; however, a systematic perturbation of heme B1g vibrational frequencies was found in the oxidized holoprotein. The heme vibrational frequencies of c552 are compared to those of the diheme peptide and of other c-type cytochromes. They are consistent with an interpretation that involves pH-dependent changes in axial ligation and treats the hemes and flavin as isolated chromphores communicating via protein-mediated interactions.