A resonant two-photon ionization study of the jet-cooled RuC molecule has identified the ground state as a Σ+1 state arising from the 10σ211σ25π42δ4 configuration. The Δi3 state arising from the 10σ211σ25π42δ312σ1 configuration lies very low in energy, with the Δ33 and Δ23 components lying only 76 and 850 cm−1 above the ground state, respectively. Transitions from the X 1Σ+, Δ33, and Δ23 states to the Π23, Π13, Φ33, Φ43, Φ31, and Π11 states arising from the 10σ211σ25π42δ36π1 configuration have been observed in the 12 700–18 100 cm−1 range, allowing all of these states to be placed on a common energy scale. The bond length increases as the molecule is electronically excited, from r0=1.608 Å in the 2δ4, X 1Σ+ state, to 1.635 Å in the 2δ312σ1, Δ3 state, to 1.66 Å in the 2δ36π1, Π3 and Φ3 states, to 1.667 Å in the 2δ36π1, Φ1 and 1.678 Å in the 2δ36π1, Π1 state. A related decrease in vibrational frequency with electronic excitation is also observed. Hyperfine splitting is observed in the 2δ312σ1, Δ33 state for the Ru99(I=5/2)12C and Ru101(I=5/2)12C isotopic combinations. This is analyzed using known atomic hyperfine parameters to show that the 12σ orbital is roughly 83% 5sRu in character, a result in good agreement with previous work on the related RhC and CoC molecules.

Proteins are separated by size exclusion chromatography while atomic ions from the inorganic elements are detected on-line by inductively coupled plasma-mass spectrometry. A double focusing mass analyzer provides very high sensitivity, low background, and sufficient spectral resolution to separate the atomic ions of interest from most polyatomic ions at the same nominal m/z value. The chromatograms show the distribution of the elements of interest between protein-bound and free fractions and provide the approximate molecular weights of those protein fractions that contain the elements monitored. The distribution of various elements, including V, Mo, Fe, Co, Mn, and lanthanides, in human or bovine serum samples are shown. Alkali metals and Tl are present primarily as free metal ions and are not bound to proteins. Inorganic elements spiked into the serum samples can be followed into various proteins. EDTA does not remove Fe, Pb, Sn, or Th from the proteins but does extract Mn from some proteins. Procedures for determining the effects of breaking disulfide linkages on the metal binding characteristics of proteins are also described.

A general method to identify trace elements in biological molecules is described. These measurements are made in only a few minutes without preliminary isolation and preconcentration steps. Many unusual or difficult elements, such as Cr, Se, Cd, Th, and U, can be observed at ambient levels bound to proteins in human serum. A new protein or family of proteins, that either contain Se or that bind Se molecules, is found with molecular weight ∼ 760 kDa. Binding of metal cations to DNA restriction fragments can be studied by similar procedures both for essential elements such as Mn and Fe and toxic ones such as Cd and Pb. In particular, trace Pb, Cd, and Co are completely bound to DNA fragments. Reduction of chromate to a cation (probably Cr 3+ ) and subsequent binding of the Cr cation to DNA is also demonstrated.