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Wyszukujesz frazę "electron paramagnetic resonance" wg kryterium: Temat


Wyświetlanie 1-4 z 4
Tytuł:
Mitochondria recycle nitrite back to the bioregulator nitric monoxide.
Autorzy:
Nohl, Hans
Staniek, Katrin
Sobhian, Babak
Bahrami, Soheyl
Redl, Heinz
Kozlov, Andrey
Powiązania:
https://bibliotekanauki.pl/articles/1044210.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
nitrite reductase
electron paramagnetic resonance
nitric oxide
mitochondria
Opis:
Nitric monoxide (NO) exerts a great variety of physiological functions. L-Arginine supplies amino groups which are transformed to NO in various NO-synthase-active isoenzyme complexes. NO-synthesis is stimulated under various conditions increasing the tissue of stable NO-metabolites. The major oxidation product found is nitrite. Elevated nitrite levels were reported to exist in a variety of diseases including HIV, reperfusion injury and hypovolemic shock. Denitrifying bacteria such as Paracoccus denitrificans have a membrane bound set of cytochromes (cyt cd1, cyt bc) which were shown to be involved in nitrite reduction activities. Mammalian mitochondria have similar cytochromes which form part of the respiratory chain. Like in bacteria quinols are used as reductants of these types of cytochromes. The observation of one-e- divergence from this redox-couple to external dioxygen made us to study whether this site of the respiratory chain may also recycle nitrite back to its bioactive form NO. Thus, the aim of the present study was therefore to confirm the existence of a reductive pathway which reestablishes the existence of the bioregulator NO from its main metabolite NO2-. Our results show that respiring mitochondria readily reduce added nitrite to NO which was made visible by nitrosylation of deoxyhemoglobin. The adduct gives characteristic triplet-ESR-signals. Using inhibitors of the respiratory chain for chemical sequestration of respiratory segments we were able to identify the site where nitrite is reduced. The results confirm the ubiquinone/cyt bc1 couple as the reductant site where nitrite is recycled. The high affinity of NO to the heme-iron of cytochrome oxidase will result in an impairment of mitochondrial energy-production. "Nitrite tolerance" of angina pectoris patients using NO-donors may be explained in that way.
Źródło:
Acta Biochimica Polonica; 2000, 47, 4; 913-921
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
In vitro effects of ozone on human erythrocyte membranes: An EPR study
Autorzy:
Górnicki, Albert
Gutsze, Aleksander
Powiązania:
https://bibliotekanauki.pl/articles/1044218.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
spin labelling
erythrocyte membrane fluidity
electron paramagnetic resonance
medical ozone
Opis:
The effects of ozone at different concentrations (10, 30, 45 g/m3) on fluidity and thermotropic properties of erythrocyte membranes were investigated by EPR using two spin probes: 5-doxylstearic acid (5-DSA) and 16-doxylstearic acid (16-DSA). The effect of ozone on the erythrocyte membrane fluidity was a dose-dependent process. The ozone at concentration of 10 g/m3 caused rigidization of the membrane while at concentration of 45 g/m3 increased fluidity both on the surface and in the deeper hydrocarbon region of the membrane. Temperature transitions close to the polar heads region (monitored by 5-DSA) were not sensitive to an increase in ozone concentration. In the case of 16-DSA, low temperature thermotropic transition (around 20°C) gradually decreased with the increase of ozone concentration. High temperature transition (around 40°C) significantly differed at the ozone concentration of 10 g/m3 and 45 g/m3, being higher and lower, respectively, as compared to untreated cells. For the ozone concentration of 45 g/m3 the disappearance of the low temperature break and the appearance of two breaks at 37°C and 16°C were observed.
Źródło:
Acta Biochimica Polonica; 2000, 47, 4; 963-971
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Attaching a spin to a protein - site-directed spin labeling in structural biology
Autorzy:
Czogalla, Aleksander
Pieciul, Aldona
Jezierski, Adam
Sikorski, Aleksander
Powiązania:
https://bibliotekanauki.pl/articles/1041067.pdf
Data publikacji:
2007
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
protein structure
site-directed spin labeling
electron paramagnetic resonance (EPR) spectroscopy
Opis:
Site-directed spin labeling and electron paramagnetic resonance spectroscopy have recently experienced an outburst of multiple applications in protein science. Numerous interesting strategies have been introduced for determining the structure of proteins and its conformational changes at the level of the backbone fold. Moreover, considerable technical development in the field makes the technique an attractive approach for the study of structure and dynamics of membrane proteins and large biological complexes at physiological conditions. This review focuses on a brief description of site-directed spin labeling-derived techniques in the context of their recent applications.
Źródło:
Acta Biochimica Polonica; 2007, 54, 2; 235-244
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Probing iso-1-cytochrome c structure by site-directed spin labeling and electron paramagnetic resonance techniques
Autorzy:
Pyka, Janusz
Osyczka, Artur
Turyna, Bohdan
Blicharski, Wojciech
Froncisz, Wojciech
Powiązania:
https://bibliotekanauki.pl/articles/1044446.pdf
Data publikacji:
1999
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
iso-1-cytochrome c
Saccharomyces cerevisiae
site-directed mutagenesis
spin label
electron paramagnetic resonance
Opis:
A cysteine-specific methanethiosulfonate spin label was introduced into yeast iso-1-cytochrome c at three different positions. The modified forms of cytochrome c included: the wild-type protein labeled at naturally occurring C102, and two mutated proteins, S47C and L85C, labeled at positions 47 and 85, respectively (both S47C and L85C derived from the protein in which C102 had been replaced by threonine). All three spin-labeled protein derivatives were characterized using electron paramagnetic resonance (EPR) techniques. The continuous wave (CW) EPR spectrum of spin label attached to L85C differed from those recorded for spin label attached to C102 or S47C, indicating that spin label at position 85 was more immobilized and exhibited more complex tumbling than spin label at two other positions. The temperature dependence of the CW EPR spectra and CW EPR power saturation revealed further differences of spin-labeled L85C. The results were discussed in terms of application of the site-directed spin labeling technique in probing the local dynamic structure of iso-1-cytochrome c.
Źródło:
Acta Biochimica Polonica; 1999, 46, 4; 889-899
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-4 z 4

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