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EN
The ^{57}Fe, ^{119}Sn, ^{129}I, and ^{151}Eu Mössbauer spectroscopy, scanning force microscopy, and optical fluorescence method were applied to study biological systems starting from porphyrins, through cytochromes and cell membranes until such a complex system as photosystem II. In Fe-porphyrin aggregates iron atoms are able to trap an electron exhibiting the mixed valence Fe^{3+}-Fe^{2+} relaxation process. In ironcytochrome c the presence of two different Fe^{3+} states are indicated, while in tincytochrome Sn appears in Sn^{4+} and Sn^{2+} states. From the temperature dependence of the mean square displacement of the resonance nuclei and from the diffusional broadening of the Mössbauer line it was possible to separate the vibrational, fast collective and slow collective motions in tinporphyrin and in iron- and tin-cytochrome c. The electronic state of iodine in oleic acid, the main constituent of cellular membranes, was determined. The molecular mechanism of triphenyltin interaction with membrane of red blood cells has been suggested and the model of haemolysis has been proposed. In photosystem II, Eu ions replacing calcium showed Eu^{3+} to Eu^{2+} transition after illumination with light, which points out the possible role of Ca^{2+} ions in electron transfer in the process of photosynthetic water splitting process.
EN
Mössbauer spectroscopy was applied, for the first time, to study the interaction of copper ions with the non-heme iron and the heme iron of cytochrome b_{559} in photosystem II thylakoids isolated from a Chlamydomonas reinhardtii photosystem I minus mutant. We showed that copper ions oxidize the heme iron and change its low spin state into a high spin state. This is probably due to deprotonation of the histidine coordinating the heme. We also found that copper preserves the non-heme iron in a low spin ferrous state, enhancing the covalence of iron bonds as compared to the untreated sample. We suggest that a disruption of hydrogen bonds stabilizing the quinone-iron complex by Cu^{2+} is the mechanism responsible for a new arrangement of the binding site of the non-heme iron leading to its more "tense" structure. Such a diamagnetic state of the non-heme iron induced by copper results in a magnetic decoupling of iron from the primary quinone acceptor. These results indicate that Cu does not cause removal of the non-heme iron from its binding site. The observed Cu^{2+} action on the non-heme iron and cytochrome b_{559} is similar to that previously observed forα-tocopherol quinone.
EN
Since the dawn of the 21st century, pharmacology has become a field increasingly closely related to the development of a new science - genomics. Due to increasingly smaller efficacy of using 'conventional' therapies, the world of science is starting to seek drugs dedicated to patients with a specific genotype. The possibility of finding the genetic background of diseases largely incurable to this date, such as cancers, diabetes or depression, will allow for ?targeted therapy', improving thereby therapy efficacy by adjusting optimum treatment agents to the individual genetic profile of a specific patient. With propagation of this new type of medicine ? personalized medicine, the approach to therapy and the attitude of the patient himself are changing, as the patient seeing efficacy of his therapy is more willing to closely cooperate with the managing physician. Considerations discussed therein allow for a conclusion that further pharmacogenetic research is necessary not only to improve therapy efficacy, but also to seek possibilities of reasonable cost savings in medicine.
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