Tyrosine phenoxyl radical (TyrO*) has been detected recently in a number of proteins by comparing experimentally observed electron paramagnetic resonance, UV resonance Raman, or Fourier transform IR vibrational spectra with the corresponding spectra for the organic phenoxyl radical (PhO"). Density-functional calculations are described to illustrate the strengths and limitations of the phenoxyl radical model for the structures, electronic spin densities, vibrational frequencies, and vibrational modes of TyrO*. Both the PhO* and TyrO* radicals display substantial C=0 double bond character, whereas distances within the carbon ring are intermediate between distances observed for the corresponding bonds of phenol and p-benzoquinone. The striking structural similarity between the two radicals appears despite the proximity of the CO2H and NH2 groups located gauche to the phenoxyl side chain of TyrO" in the amino acid radical's most stable calculated gas-phase conformation. Electronic spin densities calculated for the atoms of both PhO* and TyrO* agree well with experimentally derived spin density ratios and display a pattern characteristic of odd-alternant hydrocarbons. Calculated spin densities for the two radicals differ from each other by less than 0.03, implying that the unpaired electron of TyrO* resides entirely on its phenoxyl side chain. Calculated, harmonic vibrational frequencies for both PhO* and TyrO* are within -3.3% to +3.9% of experimentally determined frequencies. Most vibrational frequencies and modes involving motions within the ring planes of PhO* and TyrO* are also very similar to each other. The largest frequency shifts upon replacing the hydrogen of PhO* with the peptide chain of TyrO* can be attributed to two effects: (1) the different bonding and mass of the peptide chain compared to the hydrogen it replaces in PhO* and (2) interactions between the TyrO* peptide chain and its phenoxyl side chain. TyrO* modes with the largest mixing between peptide chain and phenoxyl side chain motions are identified, as they are likely to be most sensitive to TyrO* conformation and offer the best potential for studying subtle conformational differences between TyrO* radicals in different proteins. Calculated isotopic frequency shifts for TyrO*-¿7 and TyrO*-,JC6 are also reported to aid in mode assignments. Furthermore, the C^O'' stretching mode is the only mode of TyrO*-,sO'? and TyrO"-,JC¿: calculated to appear above 1350 cm-1 that displays a substantial isotopic frequency shift (-24 and -37 cm-1, respectively). Thus, the C^O^s tretching mode may be identified by either lsO'' or 13C? isotopic substitution experiment.

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Combining nonequilibrium Green’s function technique with density functional theory, the electronic structure−transport property relationships of polyferrocenylene, polyferrocenylacetylene, and polyferrocenylsilane were comparatively studied. We have found that the bridge group between two adjacent ferrocene units plays an important role in tuning their conductivity. The conductivity follows the sequence polyferrocenylene, polyferrocenylacetylene, and polyferrocenylsilane, in agreement with the experimental observation. The sequence cannot be interpreted by different band gaps; electronic structure factors such as Fe−Fe, Fe−cyclopentadienyl, and cyclopentadienyl−bridge group interactions, which influence the conductivity, are identified.