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Wyszukujesz frazę "Burda, K." wg kryterium: Wszystkie pola


Wyświetlanie 1-2 z 2
Tytuł:
Application of Mössbauer Spectroscopy in Study of Selected Biochemical Processes
Autorzy:
Burda, K.
Stanek, J.
Powiązania:
https://bibliotekanauki.pl/articles/2035750.pdf
Data publikacji:
2003-05
Wydawca:
Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:
82.80.Ej
82.39.Jn
82.35.Np
82.39.Wj
82.39.Rt
Opis:
The $\text{}^{57}$Fe, $\text{}^{119}$Sn, $\text{}^{129}$I, and $\text{}^{151}$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$\text{}^{3+}$-Fe$\text{}^{2+}$ relaxation process. In ironcytochrome c the presence of two different Fe$\text{}^{3+}$ states are indicated, while in tincytochrome Sn appears in Sn$\text{}^{4+}$ and Sn$\text{}^{2+}$ 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$\text{}^{3+}$ to Eu$\text{}^{2+}$ transition after illumination with light, which points out the possible role of Ca$\text{}^{2+}$ ions in electron transfer in the process of photosynthetic water splitting process.
Źródło:
Acta Physica Polonica A; 2003, 103, 5; 499-509
0587-4246
1898-794X
Pojawia się w:
Acta Physica Polonica A
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Mössbauer Studies of Cu(II) Ions Interaction with the Non-Heme Iron and Cytochrome b$\text{}_{559}$ in a Chlamydomonas reinhardtii PSI Minus Mutant
Autorzy:
Burda, K.
Kruk, J.
Strzałka, K.
Stanek, J.
Schmid, G. H.
Kruse, O.
Powiązania:
https://bibliotekanauki.pl/articles/2044646.pdf
Data publikacji:
2006-03
Wydawca:
Polska Akademia Nauk. Instytut Fizyki PAN
Tematy:
82.39.Jn
82.39.Rt
82.50.Nd
87.15.He
87.64.Pj
89.60.Fe
Opis:
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$\text{}_{559}$ 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$\text{}^{2+}$ 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$\text{}^{2+}$ action on the non-heme iron and cytochrome b$\text{}_{559}$ is similar to that previously observed forα-tocopherol quinone.
Źródło:
Acta Physica Polonica A; 2006, 109, 3; 237-247
0587-4246
1898-794X
Pojawia się w:
Acta Physica Polonica A
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-2 z 2

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