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1.
Int J Syst Evol Microbiol ; 68(3): 871-875, 2018 Mar.
Article in English | MEDLINE | ID: mdl-29458537

ABSTRACT

An anaerobic sulfate-reducing micro-organism, strain 3408-1T, was isolated from a terrestrial hot spring in Kamchatka peninsula (Russia). The cells were spore-forming rods with a Gram-positive type of cell wall. The new isolate was a moderately thermoacidophilic anaerobe able to grow either by sulfate or thiosulfate respiration with H2 or formate as substrates, or by fermenting yeast extract, maltose, sucrose, glucose and pyruvate. The fermentation products were acetate, CO2 and H2. The pH range for growth was 2.9-6.5, with an optimum at 4.5. The temperature range for growth was 42-70 °C, with an optimum at 55 °C. The G+C content of DNA was 58 mol%. Phylogenetic analysis of the 16S rRNA gene showed that strain 3408-1T belongs to the family Thermoanaerobacteraceae, order Thermoanaerobacterales and was distantly related to the species of the genus Ammonifex(93-94 % sequence similarity). On the basis of physiological properties and results of phylogenetic analysis, strain 3408-1T is considered to represent a novel species of a new genus, for which the name Desulfothermobacter acidiphilus gen. nov., sp. nov. is proposed. The type strain is 3408-1T (=DSM 105356T=VKM B-3183T).


Subject(s)
Firmicutes/classification , Hot Springs/microbiology , Phylogeny , Bacterial Typing Techniques , Base Composition , DNA, Bacterial/genetics , Fatty Acids/chemistry , Fermentation , Firmicutes/genetics , Firmicutes/isolation & purification , Oxidation-Reduction , RNA, Ribosomal, 16S/genetics , Russia , Sequence Analysis, DNA , Sulfates/metabolism
2.
Eur Biophys J ; 19(5): 253-6, 1991.
Article in English | MEDLINE | ID: mdl-2060496

ABSTRACT

Rats have been enriched in 57Fe and erythrocytes were isolated from the blood. Mössbauer absorption spectroscopy on the hemoglobin of these erythrocytes has shown rather similar dynamics as found earlier in crystals of myoglobin, in frozen solutions of human hemoglobin and in a number of other proteins. The results strongly indicate that the motion of the heme and presumably some part of the F-helix is mainly influenced by the average viscosity of the sample determined by a network of hydrogen bridges and other weak interactions. Extrapolations of Mössbauer results from protein crystals to proteins in their physiological surroundings seem to be suitable for heme proteins.


Subject(s)
Erythrocytes/metabolism , Hemoglobins/metabolism , Animals , Heme/metabolism , Hemoglobins/chemistry , Iron/metabolism , Kinetics , Protein Conformation , Rats , Spectroscopy, Mossbauer
3.
Mol Biol (Mosk) ; 17(3): 532-42, 1983.
Article in Russian | MEDLINE | ID: mdl-6877231

ABSTRACT

A review of the recent data on protein dynamics (mainly myoglobin) by X-ray technique, Mössbauer spectroscopy and Rayleigh scattering of Mössbauer radiation is given. The connection between dynamical and functional properties of biological systems are discussed.


Subject(s)
Protein Conformation , Proteins/metabolism , Animals , Kinetics , Myoglobin/metabolism , Spectrum Analysis/methods , Temperature , X-Ray Diffraction/methods
4.
Biofizika ; 28(1): 131-3, 1983.
Article in Russian | MEDLINE | ID: mdl-6600939

ABSTRACT

Mobility of the Mössbauer label attached to the membrane proteins and the Mössbauer probe embedded into the lipid matrix of the bacterial chromatophores were studied. Positive correlation was established between the dynamic properties of hydrophobic compartments in the chromatophores and functional electron--transport activity at the level of quinone cofactors associated with the photosynthetic reaction centres.


Subject(s)
Bacterial Chromatophores/ultrastructure , Intracellular Membranes/ultrastructure , Membrane Proteins/analysis , Rhodobacter sphaeroides/ultrastructure , Electron Transport , Spectrum Analysis/methods
6.
Proc Natl Acad Sci U S A ; 77(12): 7218-21, 1980 Dec.
Article in English | MEDLINE | ID: mdl-6938968

ABSTRACT

New experimental data [Berg, A. I., Noks, P. P., Kononenko, A. A., Frolov, E. N., Khrymova, I. N., Rubin A. B., Likhtenstein, G. I., Goldanskii, V. I., Parak, F., Bukl, M. & Mössbauer, R. (1979) Mol. Biol. (USSR) 13, 81-89; Berg, A. I., Noks, P. P., Kononenko, A. A., Frolov, E. N., Uspenskaya, N. Y., Khrymova, I. N., Rubin, A. B., Likhtenstein, G. I. & Hideg, K. (1979) Mol. Biol (USSR) 13, 469-477] provide evidence that the electron tunneling process is connected to a special type of conformational transition (segmental transition) protein macromolecules in photosynthetic membranes. This problem is investigated with a simple mechanical model. It is shown that the segmental degree of freedom can play the role of the strongly interacting accepting mode for the electron tunneling process. The temperature dependences of the electron tunneling rate and the recoilless gamma-ray absorption of membrane-bound 57Fe, as an indicator of the intramolecular mobility, are calculated. The problem of energy storage in proteins is also discussed.


Subject(s)
Electrons , Proteins/physiology , Biophysical Phenomena , Biophysics , Energy Transfer , Iron , Macromolecular Substances , Membrane Proteins , Models, Biological , Motion , Protein Conformation , Thermodynamics
8.
Biofizika ; 24(3): 519-23, 1979.
Article in Russian | MEDLINE | ID: mdl-223658

ABSTRACT

Temperature relationship of rotation diffusion parameters of radical connected to different varieties of cotton filament, isolated from normal and with affected cotton was studied. It has been found that structural transitions accompanied with a markable increase of radical rotation diffusion in all the samples studied, proceed at definite temperatures. For filament samples from wilt-affected plants temperatures at which structural transitions proceed are higher as compared to the filaments taken from normal plants. This phenomenon point to higher micro rigidity of wilt-affected plants.


Subject(s)
Gossypium , Species Specificity , Climate , Electron Spin Resonance Spectroscopy , Plant Diseases , Soil , Tajikistan , Temperature
9.
Mol Biol (Mosk) ; 13(3): 567-76, 1979.
Article in Russian | MEDLINE | ID: mdl-460202

ABSTRACT

The mobility of separate sites of the water-protein matrix depending on temperature and degree of hydration has been investigated by means of spin labels covalently attached to surface layers of proteins (alpha-chymotrypsin and human serum albumin) and also by a spin probe in a hydrophobic "pocket" of human serum albumin. The results obtained are compared with the data on the mobility of gamma-resonance labels (57Fe) firmly bound with the protein matrix in the same samples. At certain temperature and degree of hydration both spin and gamma-resonance label show an increase in mobility. With the degree of hydration increasing one may observe a simultaneous increase in energy and in entropy of activation: rotatory diffusion of spin labels, i. e., a compensation effect takes place which confirms the concept expressed earlier that cooperation of water-protein interactions is the main reason of CEF. It should be noted that at P/PS greater than 0.8 the values of delta E =7 divided by 10 kcal/mole, and delta S not equal to = 9 divided by 11 e. e. are specific to glycerol-like systems, i. e., under these conditions (P/Ps greater than 0.8) the water-protein layer has glycerol-like properties.


Subject(s)
Chymotrypsin , Serum Albumin, Bovine , Spin Labels , Calorimetry , Hydrogen Bonding , Kinetics , Protein Binding , Temperature
10.
Mol Biol (Mosk) ; 13(2): 443-9, 1979.
Article in Russian | MEDLINE | ID: mdl-220524

ABSTRACT

The possibility of using gamma resonance spectroscopy (GRS) for studying the dynamics of water-protein systems is shown in the present work. The experiments were carried out on an albumin-water system. The results obtained are compared with those obtained by the spin label method under the same conditions. The different behaviour of Fe ions which are firmly- and weakly-related with the protein matrix allows to separate the mobility of the whole protein macromolecule and also the mobility of its subunits.


Subject(s)
Serum Albumin , Chemical Phenomena , Chemistry , Electron Spin Resonance Spectroscopy , Humans , Iron , Solutions , Spectrometry, Gamma , Temperature , Water
11.
Mol Biol (Mosk) ; 13(2): 469-77, 1979.
Article in Russian | MEDLINE | ID: mdl-220525

ABSTRACT

In pigment-protein complexes of photosynthetic reaction centres (RC's), extracted from chromatophore membranes of Rps. sphaeroides with sodium dodecylsulphate, functional activity and intramolecular mobility were studied as a function of temperature and hydration by use of the technique of optical absorbance and ESR spectroscopy. Over the studied temperature range from +20 to -120 degrees C and at a relative humidity (P/Ps) from 0.9 to 0.1, there observed a close interrelationship between reversible kinetic changes of direct and backward redox-reactions of the photo-reduced endogeneous acceptor of quinone nature and the effective parameter of the correlation time of the rotational diffusion of the hydrophobic spin probe as well as of spin labels chemically bound to SH- and COOH-groups of amino acid residues of the RC's protein. The findings support the view that the conformational dynamics in the RC controls the effectiveness of the primary processes of stabilization of photochemically separated charges.


Subject(s)
Photosynthesis , Rhodobacter sphaeroides , Bacterial Chromatophores , Bacterial Proteins , Binding Sites , Chemical Phenomena , Chemistry , Electron Spin Resonance Spectroscopy , Molecular Conformation , Oxidation-Reduction , Spectrum Analysis , Temperature , Water
12.
Mol Biol (Mosk) ; 13(1): 81-9, 1979.
Article in Russian | MEDLINE | ID: mdl-111034

ABSTRACT

In reaction centres of photosynthetic membranes of R, rubrum the efficiency of redox interactions of the photoreduced primary electron acceptor with secondary acceptors and photooxidized bacteriochlorophyll has a marked and reversible dependence on temperature over the range from -20 degrees to -80 degrees. Similar temperature dependences were observed for correlation times of the rotational diffusion of a spin probe bound to the hydrophobic region of the membrane and of a spin label bound to SH-groups of the protein constituent of the membrane, as well as for characteristics of resonance absorption of the Mössbauer probe (57Fe), embedded in the membrane by biosynthesis. Using the same indicators of intramolecular mobility, a correlation has been observed between photoactivity and structure of the membrane in experiments involving hydratation changes of samples. The data suggest the existence of a close interrelationship between the conformational mobility of the constituents of the photosynthetic membrane and their specific reaction capacity.


Subject(s)
Bacteriorhodopsins , Carotenoids , Photosynthesis , Rhodospirillum rubrum/metabolism , Bacteriochlorophylls/metabolism , Bacteriorhodopsins/metabolism , Carotenoids/metabolism , Electron Transport , Kinetics , Oxidation-Reduction , Protein Conformation , Spectrum Analysis
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