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1.
Biofizika ; 46(5): 859-61, 2001.
Article in Russian | MEDLINE | ID: mdl-11605386

ABSTRACT

An explanation of the appearance of the reproducible fine structure of the histograms corresponding to different processes from simple chemical reactions to radioactive decays is developed. Earlier this explanation was reduced to extremely strong influence of small changes between energy levels of a quantum system under study and its environment on the transition probability of the system (chemical reaction, radioactive decay, e.t.c.) from the system last quantum state to final result of the studied process. In the present paper it is supposed that the main factors determining this probability is the periodical or quasi-periodical low frequency changes of local gravitational field leading to corresponding changes of the system mass (the quantum transition probability depends exponentially on the latter). This approach seems to able to propose non-contradictory explanation of many manifestations of macroscopic fluctuation.


Subject(s)
Extraterrestrial Environment , Periodicity , Quantum Theory , Alpha Particles , Physical Phenomena , Physics , Radioactivity , Statistical Distributions
2.
Biofizika ; 44(1): 59-65, 1999.
Article in Russian | MEDLINE | ID: mdl-10330582

ABSTRACT

The analysis of the saturation curves of ESR signals revealed a decrease in the relaxation rate of fast-relaxation Cu(I) complexes on the cytoplasmic membrane of E. coli after the interaction of these bacteria with low concentrations of SH-reagents. It was concluded that the observed changes are associated with the reorganization of Cu clusters due to the binding of SH groups incorporated into the clusters N-ethylmaleimide or Ag(I).


Subject(s)
Copper/metabolism , Cytoplasm/metabolism , Escherichia coli/metabolism , Sulfur/metabolism , Cell Membrane/metabolism , Electron Spin Resonance Spectroscopy , Ethylmaleimide/chemistry , Ligands , Silver/chemistry , Sulfhydryl Reagents/chemistry , Sulfhydryl Reagents/metabolism
3.
Biofizika ; 40(2): 383-8, 1995.
Article in Russian | MEDLINE | ID: mdl-7578343

ABSTRACT

Experiments on semisynchronized cultures of animal and plant cells, performed in our laboratory approximately 30 years ago, have demonstrated that there exist regular changes of certain physical parameters of the cells during the cell cycle. In particular on yeast cultures there has been observed the appearance of specific electron paramagnetic resonance (EPR) signals with simultaneous change of the static magnetic susceptibility of the cultures in the period immediately preceding the beginning of the intensive budding. On chlorella cultures grown at certain regimes of light and darkness it is possible to observe characteristic changes of the kinetics of the photoconduction signal at the frequency of 10 HHz (SHR-photoconduction). It can be conjectured that these effects are of a similar nature linked to some changes of the intracellular structures at certain stages of the cell cycle. The work performed much later makes it possible to link these changes to the appearance of spin, glass-like structures in macromolecular intracellular bodies.


Subject(s)
Cell Cycle , Animals , Cells, Cultured , Electron Spin Resonance Spectroscopy , Kinetics , Magnetics , Plant Cells , Plants/chemistry
4.
Biofizika ; 38(1): 129-32, 1993.
Article in Russian | MEDLINE | ID: mdl-8471638

ABSTRACT

At extra-low concentrations of biologically active substances (BAS) the limiting stage of processes determining their action at cell and sub-sell levels is BAS diffusion to the cell surface. According to proposed parametric resonance model the BAS activity extreme values are to be observed when the reciprocal values of collision frequency between BAS molecules and cell surface coincide (by order of magnitude) with the characteristic times of conformational relaxation of certain macromolecular structures responsible of the studied process. The calculation results do not contradict the experimental data.


Subject(s)
Enzymes/physiology , Diffusion , Enzymes/chemistry , Macromolecular Substances , Protein Conformation
5.
Biofizika ; 38(1): 99-107, 1993.
Article in Russian | MEDLINE | ID: mdl-7682446

ABSTRACT

The sequence of nucleotides in a single-stranded RNA molecule is represented by a complex vector, whose k-th component corresponds to the k-th base of the sequence ordered in the 5'3' direction. An analysis of the proposed formalisms permits to predict a new type of reversible conformational transitions between the secondary structure patterns of RNA which may have an oscillatory character. A possible experimental approach based on the ESR technique for recording and time-scale estimation of these transitions is proposed.


Subject(s)
Genetic Vectors , RNA/chemistry , Electron Spin Resonance Spectroscopy , Nucleic Acid Conformation
6.
Biofizika ; 37(5): 923-6, 1992.
Article in Russian | MEDLINE | ID: mdl-1472568

ABSTRACT

With the help of retarded double-time Green function technique a method of estimation of electron transfer rate in protein macromolecules has been developed. Possible experimental test is suggested.


Subject(s)
Electron Transport , Peptides/chemistry , Kinetics , Mathematics
7.
Biofizika ; 35(1): 141-2, 1990.
Article in Russian | MEDLINE | ID: mdl-2346758

ABSTRACT

It has been shown that a fast increase in pH of myosin solution leads to ATP formation de novo from ADP and Pi (about one ATP molecule per one myosin molecule). The obligatory condition for ATP synthesis was that the value of pH 7.9-8.0 should be crossed in the course of pH-jump. The data obtained are explained in terms of the concept of conformational relaxation in enzyme catalysis.


Subject(s)
Adenosine Triphosphate/biosynthesis , Muscles/metabolism , Myosins/metabolism , Animals , Hydrogen-Ion Concentration , Hydrolysis , Kinetics , Rabbits
8.
Biofizika ; 34(4): 630-4, 1989.
Article in Russian | MEDLINE | ID: mdl-2553129

ABSTRACT

Correlation between cell cycle of the synchronous yeast culture and ESR signal intensity at g 2.2 and 77 K was studied. It was shown that the maximal intensity of ESR signal was reached 10-15 min before the beginning of intensive cell division. The ESR signal with g 2.2 (77 K) is caused by the spin-glass like structure. The "freezing" temperature of these spin-glasses was measured.


Subject(s)
Magnetics , Saccharomyces cerevisiae/growth & development , Cell Division , Electron Spin Resonance Spectroscopy
9.
Biofizika ; 32(5): 800-13, 1987.
Article in Russian | MEDLINE | ID: mdl-2891381

ABSTRACT

An "elementary act" of ATP formation from ADP and Pi in energy-transducing organels (mitochondria, chloroplasts and chromatophores) can be realized without closed membrane vesicles, pieces of membranes and F0-component of H+ATPase. The "elementary act" is initiated by a rather fast deprotonation of several acid groups of the coupling factor F1 (or CF1), this process leads to structurally non-equilibrium state of the enzyme due to the appearance of "additional" negative charges in unchanged protein globula. The endergonic step of ATP synthesis, i. e. release of tightly-bound ATP into the aqueous medium, occurs during conformational relaxation of the non-equilibrium state of H+ATPase. Closed membrane vesicles are necessary for a cyclic return of the enzyme to the initial state with protonized functional groups, this provides multiple synthesis of ATP under the steady state and quasi-stationary conditions. The energetical aspects and details of possible schemes of ATP synthesis initiated by artificial electrochemical gradient of protons, as well as ATP formation during oxidative and photophosphorylation are discussed here.


Subject(s)
Adenosine Triphosphate/biosynthesis , Cell Membrane/metabolism , Energy Metabolism , Animals , Cell Membrane/enzymology , Models, Biological , Proton-Translocating ATPases/metabolism
10.
Biofizika ; 31(5): 760-3, 1986.
Article in Russian | MEDLINE | ID: mdl-3778953

ABSTRACT

Changes in the duration of self tryptophane fluorescence of soluble cytoplasmic malate dehydrogenase (MDG) and kinetics of chemical transformation in the course of single cycles of direct and reversible reaction L-malate in equilibrium with oxalacetate were recorded. MDG was shown to catalyse the direct and reversible reactions at different conformational states. The reaction coordinates for direct and reversible processes do not coincide in this case.


Subject(s)
Malate Dehydrogenase/metabolism , Animals , Kinetics , Models, Biological , Myocardium/enzymology , Protein Conformation , Spectrometry, Fluorescence , Swine
12.
Biofizika ; 30(4): 703-4, 1985.
Article in Russian | MEDLINE | ID: mdl-2996621

ABSTRACT

Interaction between methemoglobin and cyanide was studied by low temperature inhibition method in combination with ESR. A new, not earlier described in literature ESR signal of low spin cyanide complex of this protein was recorded.


Subject(s)
Cyanides/metabolism , Methemoglobin/metabolism , Electron Spin Resonance Spectroscopy , In Vitro Techniques , Kinetics
13.
Biofizika ; 29(4): 633-6, 1984.
Article in Russian | MEDLINE | ID: mdl-6091784

ABSTRACT

The dramatic diminishing of the concentration of the N-2 iron-sulfur centre of NADH-dehydrogenase of mitochondria during the growth of cell culture of hamster fibroblasts with the subsequent recovery of concentration to the initial level was discovered by means of low-temperature ESR spectroscopy. It was concluded that the results obtained are due mainly to the decrease of the number of respiratory chains, but not to the change of the electron transport chain structure.


Subject(s)
Iron-Sulfur Proteins/metabolism , Metalloproteins/metabolism , Mitochondria/metabolism , Animals , Binding Sites , Cells, Cultured , Cricetinae , Cricetulus , Electron Spin Resonance Spectroscopy , Electron Transport , Fibroblasts/metabolism , NADH Dehydrogenase/metabolism , Oxidation-Reduction
14.
Biofizika ; 29(3): 506-15, 1984.
Article in Russian | MEDLINE | ID: mdl-6087931

ABSTRACT

The data on the action of the iron-sulfur centre N-2 in the 1 site of respiration and oxidative phosphorylation coupling obtained by the authors as well as by other investigators are reviewed in terms of conformational - relaxation concept of energy transformation. The study of the direct and reverse electron transport bears testimony to the fact that the N-2 centre with its proper protein surrounding plays the role of the protein transformer of energy in the 1 site.


Subject(s)
Cytochrome Reductases/metabolism , Energy Metabolism , Iron-Sulfur Proteins/metabolism , Metalloproteins/metabolism , Mitochondria/enzymology , NADH Dehydrogenase/metabolism , Allosteric Regulation , Animals , Binding Sites , Electron Spin Resonance Spectroscopy , Electron Transport , Mitochondria/metabolism , Mitochondria, Liver/enzymology , Mitochondria, Liver/metabolism , Oxidation-Reduction , Protein Conformation , Rats
15.
Mol Biol (Mosk) ; 17(6): 1236-48, 1983.
Article in Russian | MEDLINE | ID: mdl-6318072

ABSTRACT

Effects of various temperatures on the rates of electron transport between two photosystems, the light-induced uptake of protons, kinetics of proton efflux from the chloroplasts in the dark and photophosphorylation were studied in isolated chloroplasts. There are correlations between the physical state of thylakoid membrane and the rates of electron- and proton transport processes. The temperature dependence of "structural" parameter (fluidity of lipids in membrane) as well as the rates of electron- and proton transport processes reveal the breaks under the same temperatures. Stimulation of photophosphorylation by temperature increasing correlates with the heat activation of chloroplasts latent ATPase due to thermoinduced structural changes in the heat activation of chloroplasts latent ATPase due to thermoinduced structural changes in the protein part of CF0-CF1 complex. The rate of photophosphorylation also correlates with the physical state of membrane lipids. Thermoinduced "melting" of the thylakoid membrane inhibits the ATP formation because of a decrease in photosystem 2 photochemical activity and stimulation of membrane conductivity for protons.


Subject(s)
Chloroplasts/metabolism , Fabaceae/metabolism , Intracellular Membranes/metabolism , Photophosphorylation , Plants, Medicinal , Chloroplasts/ultrastructure , Electron Spin Resonance Spectroscopy , Electron Transport , Kinetics , Protons , Temperature
16.
Biofizika ; 28(4): 606-11, 1983.
Article in Russian | MEDLINE | ID: mdl-6615899

ABSTRACT

A dramatic decrease of the rate of transport of reducing equivalents from NADH to coenzyme Q was observed in the 4th metabolic state (by Chance). It was suggested that this decrease is due to the increase of total time of transition from the structural nonequilibrium state to the equilibrium one of the N-2 center. The structural nonequilibrium state of the center N-2 was observed only under the energy-dependent reverse electron transport, when the substrates for the reduction of coenzyme Q were used.


Subject(s)
Ascomycota/enzymology , Cytochrome Reductases/metabolism , Iron-Sulfur Proteins/metabolism , Metalloproteins/metabolism , Mitochondria, Liver/enzymology , Mitochondria/enzymology , NADH Dehydrogenase/metabolism , Saccharomycetales/enzymology , Animals , Electron Transport , Kinetics , Rats
17.
Biofizika ; 28(2): 292-7, 1983.
Article in Russian | MEDLINE | ID: mdl-6303448

ABSTRACT

The structural--equilibrium and nonequilibrium forms of the center N-2 from NADH-dehydrogenase differ in their parametres of the spin-lattice relaxation. The curves of the temperature dependence of the ESR signal intensity become the effective method of the study of the iron-sulphur proteins. The structural nonequilibrium form of the center N-2 was observed in the "4th" metabolic (by Chance) state, but equilibrium form of the center N-2 prevailed in the "3d" state or in the uncoupled state.


Subject(s)
Cytochrome Reductases/metabolism , Iron-Sulfur Proteins/metabolism , Metalloproteins/metabolism , Mitochondria, Heart/enzymology , Mitochondria, Liver/enzymology , NADH Dehydrogenase/metabolism , Animals , Cattle , Electron Spin Resonance Spectroscopy , Kinetics , Temperature
18.
Mol Biol (Mosk) ; 16(1): 183-9, 1982.
Article in Russian | MEDLINE | ID: mdl-6122158

ABSTRACT

The effect of redox and chelating reagents on the ATPase and ATP-synthetase activity in chloroplast membranes as well as the ATPase activity of isolated CF1-coupling factor from chloroplasts has been studied. The Mg2+-ATPase in thylakoid membranes and isolated Ca2+-ATPase is stimulated by dithionite. In the presence of reduced glutathione the effect of dithionite is similar to those of prolonged illumination or heating. Dichlorophenolindophenol partially inhibits this activity as well as citrate, tenoyltrifluoroacetone and the excess fo ATP. Photophosphorylation in chloroplast lamellae is inhibited with dithionite. It is suggested that the membrane bound ATPase from chloroplasts may be in two structural states which differ in their enzymic activity and in the coupling to electron transfer in membrane. The transitions between these states can be induced by redox reagents.


Subject(s)
Adenosine Triphosphatases/metabolism , Chelating Agents/pharmacology , Chloroplasts/enzymology , Ca(2+) Mg(2+)-ATPase , Calcium-Transporting ATPases/metabolism , Dithionite/pharmacology , Intracellular Membranes/enzymology , Kinetics , Oxidation-Reduction , Oxidative Phosphorylation Coupling Factors/metabolism , Photophosphorylation , Plants , Proton-Translocating ATPases
19.
Biofizika ; 26(5): 782-5, 1981.
Article in Russian | MEDLINE | ID: mdl-6797479

ABSTRACT

Using flash photolysis, horseradish peroxidase rebinding of carbon monoxide has been observed in the temperature range between 20 and -70 degrees C. A lag-period of about 50 ms immediately after photodissociation takes place. This lag-period is assumed to be due to the formation of the intermediate protein form with the low reactivity. Following rebinding is bimolecular process with the rate constant 4 x 10(3) M-1 S-1 usually observed for the peroxidase reaction with carbon monoxide. For some peroxidase molecules (about 10 per cent) rebinding of carbon monoxide is CO-concentration independent monomolecular process, which implies, apparently, ligands in these molecules do not leave the protein after photodissociation.


Subject(s)
Carbon Dioxide , Horseradish Peroxidase , Peroxidases , Carbon Dioxide/radiation effects , Chemical Phenomena , Chemistry , Horseradish Peroxidase/radiation effects , Kinetics , Light , Photolysis , Protein Binding/radiation effects , Temperature
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