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Biomedical subjects

A M Kuznetsov

Publications and source records attributed to A M Kuznetsov.

At least 19 recordsLinked to original sources
PubMed2002

[Functional organization of myogenic pacemaker of the stomach in conditions of hunger and satiation].

In chronic experiments, we have studied electrical activity of muscles of the gastro-esophageal sphincter, small curvature, corpus and antrum of the stomach in conditions of hunger, food intake behaviour and satiation of the rabbits. The aim of this study involved particularities of the electrical activity of myogenic pacemaker zone of the stomach. It has been shown that function of myogenic pacemaker of the rabbit stomach is performed by smooth muscles of the small curvature of the stomach. Pacemaker properties of muscles of the small curvature of the stomach are performed in conditions of food intake behaviour and satiation.

Action Potentials↗
PubMed2001

The use of bioluminescent biotests for study of natural and laboratory aquatic ecosystems.

A set of bioluminescent tests was developed to monitor water quality in natural and laboratory ecosystems. It consisted of four bioluminescent systems: luminous bacteria, coupled enzyme system NADH:FMN-oxidoreductase-luciferase and triplet enzyme systems with alcohol dehydrogenase and trypsin. The set of biotests was applied for a small forest pond (Siberia, Russia), laboratory microecosystems polluted with benzoquinone and a batch culture of blue-green algae. Thereby effects of natural water compared to those of models of heavy pollution and "bloom" of blue-greens on the bioluminescent tests were revealed. The set of biotests was not affected by a natural seasonal variability of water quality in the unpolluted pond, but responded to the heavy pollution and the "bloom" of blue-greens. The set of biotests could be recommended as the alarm test to control the acute toxicity of natural water bodies.

Benzoquinones↗
PubMed2001

Comparative study of effects of artificial electron donors on the AT-band of photosystem II thermoluminescence.

Extraction of the Mn-cluster from photosystem II (PS II) inhibits the main bands of thermoluminescence and induces a new AT-band at -20 degrees C. This band is attributed to the charge recombination between acceptor QA- and a redox-active histidine residue on the donor side of PS II. The effect of Mn(II) and Fe(II) cations as well as the artificial donors diphenylcarbazide and hydroxylamine on the AT-band of thermoluminescence was studied to elucidate the role of the redox-active His residue in binding to the Mn(II) and Fe(II). At the Mn/PS II reaction center (RC) ratio of 90 : 1 and Fe/PS II RC ratio of 120 : 1, treatment with Mn(II) and Fe(II) causes only 60% inhibition of the AT-band. Preliminary exposure of Mn-depleted PS II preparations to light in the presence of Mn(II) and Fe(II) causes binding of the cations to the high-affinity Mn-binding site, thereby inhibiting oxidation of the His residue involved in the AT-band formation. The efficiency of the AT-band quenching induced by diphenylcarbazide and hydroxylamine is almost an order of magnitude higher than the quenching efficiency of Mn(II) and Fe(II). Our results suggest that the redox-active His is not a ligand of the high-affinity site and does not participate in the electron transport from Mn(II) and Fe(II) to YZ. The concentration dependences of the AT-band inhibition by Mn(II) and Fe(II) coincide with each other, thereby implying specific interaction of Fe(II) with the donor side of PS II.

2,6-Dichloroindophenol↗
PubMed1999

An approach to long-range electron transfer mechanisms in metalloproteins: in situ scanning tunneling microscopy with submolecular resolution.

In situ scanning tunneling microscopy (STM) of redox molecules, in aqueous solution, shows interesting analogies and differences compared with interfacial electrochemical electron transfer (ET) and ET in homogeneous solution. This is because the redox level represents a deep indentation in the tunnel barrier, with possible temporary electronic population. Particular perspectives are that both the bias voltage and the overvoltage relative to a reference electrode can be controlled, reflected in spectroscopic features when the potential variation brings the redox level to cross the Fermi levels of the substrate and tip. The blue copper protein azurin adsorbs on gold(111) via a surface disulfide group. Well resolved in situ STM images show arrays of molecules on the triangular gold(111) terraces. This points to the feasibility of in situ STM of redox metalloproteins directly in their natural aqueous medium. Each structure also shows a central brighter contrast in the constant current mode, indicative of 2- to 4-fold current enhancement compared with the peripheral parts. This supports the notion of tunneling via the redox level of the copper atom and of in situ STM as a new approach to long-range electron tunneling in metalloproteins.

Adsorption↗
PubMed1997

Electrostatics of proteins: description in terms of two dielectric constants simultaneously.

In the semi-continuum treatment of the energetics of charge formation (or transfer) inside a protein, two components of the energy are inevitably present: the energy of interaction of the ion with the pre-existing intraprotein electric field, and the energy due to polarization of the medium by the newly formed charge. The pre-existing field is set up by charges (partial or full) of the protein atoms fixed in a definite structure. The calculation of this field involves only the electronic polarization (the optical dielectric constant epsilon(o)) of the protein because the polarization due to shifts of heavy atoms has already been accounted for by their equilibrium coordinates. At the same time, the aqueous surroundings should be described by the static constant epsilon(sw), as the positions of water molecules are not fixed. The formation of a new charge, absent in the equilibrium X-ray structure, results in shifts of electrons and polar atoms, i.e., it involves all kinds of medium polarization described by the static dielectric constant of protein epsilon(s). Thus, in calculations of the total energy, two different dielectric constants of the protein are operative simultaneously. This differs from a widely used algorithm employing one effective dielectric constant for both components of the ion's energy.

Proteins↗
PubMed1992

Bioluminescent method in studying the complex effect of sewage components.

The inhibition of bacterial luminescence has been used in testing industrial enterprises sewage. The toxicity of the sewage is less than the total toxicity of separate components due to neutralization of quinone products of polyphenol oxidation in the reactions with the other phenol components of sewage. Toxicity increase is due to their influence on the cell membrane. Studies of cell ultrastructure confirm this fact. The studied mechanism of the complex effect allowed a more accurate forecast of the ecological situation during the discharge of phenol compounds and metals. It also showed the necessity of taking into account the complex effect of sewage components on contaminant discharge into water reservoirs.

Benzoquinones↗
PubMed1987

The mechanism of cathode reduction of oxygen in a carbon carrier-laccase system.

The influence of temperature, oxygen pressure and inhibitors of laccase on the dioxygen electroreduction reaction has been examined at different solution pH. On the basis of obtained data, a reaction mechanism including electron transfer from the enzyme active site to the oxygen molecule is suggested as the slow step.

Electrochemistry↗
PubMed1981

The effect of temperature and transmembrane potentials on the rates of electron transfer between membrane-bound biological redox components.

We have investigated rate data for the temperature and free energy dependence of the primary electron-transfer processes in bacterial photosynthesis. Rather than representing the whole electronic-nuclear coupling by a frequently applied discrete single-mode model, we have incorporated a continuum of modes characterized by a certain distribution function. In this way, we can illuminate the role of both a broad distribution of low-frequency modes representing the medium and a narrow distribution representing local nuclear modes. Furthermore, it emerges from the calculations that both sets are important in the overall scheme of primary photosynthetic electron-transfer processes. By means of this model and quantum-mechanical rate theory, we can reproduce a number of important features of the primary photosynthetic processes concerning in particular the temperature (tunnelling or thermally activated nuclear motion) and free energy dependence ('normal', 'activation-less', or 'inverted' regions) of the rate constants and estimate such parameters as nuclear-reorganization energy electron-exchange integrals and electron-transfer distances. We have finally considered some of the important factors which determine the potential drop across the membrane and estimated the extent to which variations in the potential drop affect the rate constants of the electron-transfer processes.

Electron Transport↗