A pulsed high voltage was applied to logs for mushroom cultivation to investigate an effect of pulse high voltage on mushroom growth. Inductive energy storage system was utilized to construct a pulsed power generator with compact size. Copper fuse of 0.03 mm diameter was used as an opening switch to interrupt large circuit current in short time. The voltage charged in primary energy storage capacitor was multiplied using secondary energy storage inductor. The output voltage of the pulsed power generator was 120 kV with 100 ns pulse width at 14 kV charging voltage of 0.22 μF primary energy storage capacitor and 15 μH secondary energy storage inductor. This pulsed high voltage was applied to 90 cm length logs inoculated Pholiota nameko fungus. The yield of Pholiota nameko mushrooms was successfully improved with the pulse voltage stimulation. The total weight of the cropped Pholiota nameko after the pulse voltage stimulation was 6.3 kg for fifteen logs and this value was 1.5 times larger than 4.3 kg of total weight without the stimulation. The number of logs with lower than 0.27 kg cropped Pholiota nameko weight which was an average value for control group was only one in fifteen, whereas four logs in control group showed almost zero weight of cropped Pholiota nameko.
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.
After summaries on Rayleigh's distribution and Wigner's surmise, the time evolution of Rayleigh-Wigner's statistics is studied and a suitable diffusion type equation is proposed. Also the variance and kurtosis of time evolution of Rayleigh's distribution are calculated. Obtained results may be useful in description of physical, social and biological processes.
A subdiffusion process, similar to a Zeldovich-Kompaneets heat conduction process, is defined by a nonlinear diffusion equation in which the diffusion coefficient takes the form D=a(t)f^n, where a=a(t) is an external time modulation, n is a positive constant, and f=f(x, t) is a solution to the nonlinear diffusive equation. It is shown that a Zeldovich-Kompaneets solution satisfies the subdiffusion equation if a=a(t) is replaced by the mean value of a. Also, a solution to the subdiffusion equation is constructed that may be useful in description of biological, social, and financial processes.
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.
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