Raman spectroscopy of mercury(II) binding to two filamentous viruses: Ff (fd, M13, f1) and Pf1

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Abstract
Ff and Pf1 are filamentous bacteriophages. Each contains, in a central core region surrounded by protein, a circular single-stranded DNA molecule, and it is known that the DNA bases are sites of HG(II) binding. In the present study, Raman spectra were obtained for the two viruses in the presence of increasing amounts of Hg(II), with ratios (m) of Hg(II) added per nucleotide residue in the range 0 < m < 2.0. Hg(II) binding to the viruses induces Raman intensity changes in previously assigned Raman lines of viral DNA, demonstrating metal binding to the DNA bases, but also in many lines assigned to protein. The overall structures of the viruses do not change with Hg(II) binding, and the Raman spectra indicate little, if any, change in protein secondary structure. Changes in certain protein Raman lines induced by Hg(II) binding to the DNA for low values of m are attributed to altered interactions between solvent and protein side chains, aliphatic groups being the most affected. The nature of such changes for both viruses suggests DNA-protein linkage. In Pf1, lines assigned to ring vibrations of all four bases are perturbed upon initial addition of Hg(II) to m = 0.25. In Ff, however, lines assigned to base ring vibrations are not perturbed until m .gtoreq. 0.5. The results provide additional evidence for fundamentally different DNA structures in Ff and Pf1.