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Quantum chemical modeling of electron paramagnetic resonance (EPR) parameters, in combination with data from the modern high-field/high-frequency EPR (HF-EPR) techniques, constitutes an invaluable analytical tool for gaining insight into radical-protein interactions, which determine the specificity and directionality of the radical-mediated biochemical processes. This thesis reports a series of density functional (DFT) studies on EPR parameters of several biologically relevant radicals and a series of molecular devices inspired by radical-protein interaction in photosystem I (PS-I). We demonstrate our methodology’s accuracy and capacity to provide insight into the in vivo environment and reactivity of bioradicals. Our DFT approach for the calculation of electronic g-tensors has been applied to semiquinone radical anions in the different protein environments of photosynthetic reaction centers. Supermolecular models have been constructed, based on combined crystallographic and quantum chemical structure data, for the QA and QB active sites of bacterial reaction centers, for the A1 site of PS-I, as well as for ubisemiquinone in frozen 2-propanol. After scaling of the computed gx components by 0.92, both gx and gy components computed at gradient-corrected DFT level with accurate spin-orbit operators agree with HF-EPR reference data essentially to within experimental accuracy in all four systems studied. The influence of the various semiquinone-protein non-covalent interactions has been studied by successive removal of individual residues from the models. The effects of hydrogen bonding to the two carbonyl oxygen atoms of the semiquinones was found to be nonadditive, due to compensating spin-polarization effects. The effects of tryptophan-semiquinone -stacking are different for QA and A1 sites. This may be traced back to a different alignment of the interacting fragments and to differential spin polarization. In the next part of this work our DFT methodology has been applied to the semiquinone in the environment of the “high-affinity” binding site of quinol oxidase (QH site). Recent multi-frequency EPR studies of the QH binding site of quinol oxidase have suggested a very asymmetric hydrogen-bonding environment for the semiquinone radical anion state. Single-sided hydrogen bonding to the O1 carbonyl position was one of the proposals, which contrasts with some previous experimental indications. The density functional calculations of the EPR parameters (g-tensors, 13C, 1H, and 17O hyperfine tensors) for a wide variety of supermolecular model complexes have been used to provide insight into the detailed relations between structure, environment and EPR parameters of ubisemiquinone radical anions. A single-sided binding model is not able to account for the experimentally observed low gx component of the g-tensor nor for the observed magnitude of the asymmetry of the 13C carbonyl hyperfine coupling (HFC) tensors. Based on the detailed comparison between computation and experiment, a model with two hydrogen bonds to O1 and one hydrogen bond to O4 was suggested for the QH site, but a model with one more hydrogen bond on each side could not be excluded. Additionally, several general conclusions on the interrelations between EPR parameters and hydrogen bond patterns of ubisemiquinones in proteins were provided. The computational studies related to the mechanism of electron transfer in PS-I gave an impetus to the theoretical design, based on quantum-chemical calculations, of relatively small rotational molecular motors made up from intramolecularly connected dyads consisting of a quinone unit and a pyrrole or indole moiety. It was shown computationally for several systems, depending on the length and attachment points of the interconnecting chains, that a reduction of the quinone to the semiquinone radical anion or quinolate dianion states leads to a reversible intramolecular reorientation from a -stacked to a T-stacked arrangement. In the rearranged structures, a hydrogen bond from the pyrrole or indole N-H function to the semiquinone or quinolate -system is created upon reduction. In some systems, hydrogen bonds to the semiquinone or quinolate oxygen atoms are partly feasible and will be preferred over T-stacking. It was shown that the intramolecular interactions modify the quinone redox potentials. The electronic g-tensors computed for the semiquinone states reflected characteristically the presence and nature of hydrogen bonds to the semiquinone and were suggested as suitable EPR spectroscopic probes for the preferred structures. Intramolecular proton transfer was observed to be possible in the dianionic state. In contrast to semiquinones, which represent paramagnetic states of enzyme cofactors, glycyl radicals are genuine protein radicals. As a step towards an in-depth understanding of the EPR parameters of glycyl radicals in proteins, the hyperfine- tensors and, particularly, the g-tensor of N-acetylglcyl in the environment of a single crystal of N-acetylglycine have been studied by systematic state-of-the-art quantum chemical calculations on various suitable model systems. The quantitative computation of the g-tensors for such glycyl-derived radicals is a veritable challenge, mainly due to the very small g-anisotropy combined with a non-symmetrical, delocalized spin-density distribution and several atoms with comparable spin-orbit contributions to the g-tensors. The choice of gauge origin of the magnetic vector potential, and of approximate spin-orbit operators, both turn out to be more critical than found in previous studies of g-tensors for organic radicals. Environmental effects, included by supermolecular hydrogen-bonded models, were found to be moderate, due to a partial compensation between the influences from intramolecular and intermolecular hydrogen bonds. The largest effects on the g-tensor are caused by the conformation of the radical. The DFT methods employed systematically overestimate both the gx and gy components of the g-tensor. This is important for investigations on the protein-glycyl radicals (see next paragraph). The 1H and 13C hyperfine couplings depend only slightly on the supermolecular model chosen and appear less sensitive probes of detailed structure and environment. The number of enzymes that require a glycyl-based radical for their function is growing. Here we provide systematic quantum-chemical studies of spin-density distributions, electronic g-tensors, and hyperfine couplings of various models of protein-bound glycyl radicals. Similarly to what was found for N-acetylglycyl (see previous paragraph), the small g-anisotropy for this delocalized, unsymmetrical system presents appreciable challenges to state-of-the-art computational methodology. This pertains to the quality of structure optimization, as well as to the choice of spin-orbit Hamiltonian and gauge origin of the magnetic vector potential. Environmental effects due to hydrogen bonding are complicated and depend in a subtle fashion on the different intramolecular hydrogen bonding for different conformations of the radical. Indeed, the conformation has the largest overall effect on the computed g-tensors (less so on the hyperfine-tensors). We discuss this in the context of different g-tensors obtained by recent HF-EPR measurements for three different enzymes. Based on results of calibration study for N-acetylglycyl, we support that the glycyl radical observed for E.coli anaerobic ribonucleotide reductase (ARNR) has a fully extended conformation, which differs from those of the corresponding radicals in pyruvate formate-lyase (PFL) or benzylsuccinate synthase (BSS).