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Biomedical subjects

G I Likhtenshteĭn

Publications and source records attributed to G I Likhtenshteĭn.

At least 19 recordsLinked to original sources
PubMed1996

[Model molybdenum-sulfur and molybdenum-iron-sulfur protein complexes].

A procedure was developed for synthesizing complexes of polynuclear molybdenum sulfide and iron-molybdenum sulfide on the basis of human serum albumin. EPR showed that molybdenum and iron atoms formed clusters in the synthesized complexes. The catalytic activity of the complexes, as determined through reaction of acetylene reduction by sodium borohydride, was significantly higher than that for previously described nonbiological systems, but lower than the characteristic values of FeMo-cofactor of nitrogenase.

Catalysis↗
PubMed1983

[Study of conformational changes in alcohol dehydrogenase during its interaction with silochrome adsorbent by the EPR spectroscopy method].

The possible use of EPR spectroscopy (spin labelling) for the study of horse liver alcohol dehydrogenase with a silochrome adsorbent is discussed. The rotatory diffusion of nitroxyl labels chemically linked to the enzyme was studied with reference to the time of the enzyme incubation with the adsorbent and the degree of its accumulation on the adsorbent surface. The mobility of nitroxyl radicals attached to the protein globules was shown to increase with time. It was concluded that the conformation of the enzyme molecules changes during their interaction with the adsorbent.

Alcohol Dehydrogenase↗
PubMed1983

[The study of the chemical composition of nitrogenase Fe-Mo-cofactor by a new fluorimetric method of thiocompound analysis].

A purification technique for a large scale production of crystalline Mo-Fe protein of nitrogenase from Azotobacter vinelandii and of its fragment, Fe-Mo-cofactor (Fe-Mo-co) in argon atmosphere has been elaborated. The novel fluorimetric method of thiol compounds analysis has been proposed for identification of Fe-Mo-co thiol ligands; this procedure allows the determination of concentration and class of thiol compounds and of the distance between sulphur atoms in the case of dithiols. The use of this method for an analysis of Fe-Mo-co has demonstrated that it contains a thiomolybdate fragment and two atoms of inorganic sulphur. Organic thiol as a Fe ligand has not been revealed.

Azotobacter↗
PubMed1977

[Study of the topography of the nitrogenase active center by the electron microscopy method with the use of the electron density labels].

The electron microscopy method has been used for studying the topography of the active centre of the nitrogenase in combination with the method of electron density labels. The active centre has been shown to place on the nitrogenase macromolecule asymmetrically. The non-heme iron atoms of the nitrogenase active centre have been regularly packed and located on the macromolecule as a quadrangular cluster closely to the surface of subunits. Two free sulfhydryl groups of the ATP-site of the nitrogenase active centre are in close proximity to the cluster. ATP-site of the nitrogenase active centre containing these groups is located on the Fe-enzyme, while the main part of the iron-containing cluster is located on the Mo-Fe-enzyme.

Adenosine Triphosphate↗
PubMedDate not supplied

[Spin label study of the surface of lipid bilayers].

The surface of liposomes and natural membranes has been studied by the method of "spin label--spin probe". Various nitroxyl radicals have been attached to membranes either dueto covalent binding with NH2-groups of phosphatidylethanolamine or due to hydrophobic interactions. Addition of paramagnetics of different charge signs (potassium ferricyanide and dibenzenechromium iodide) to spin labeled membranes results in a decrease of the EPR line intensity without marked broadening. Since the paramagnetic is attached to the membrane surface near the label it broadens the label's EPR spectrum so that it can not be observed. In this case one can observe only the spectrum of labels which have no paramagnetics in the vicinity, the nitroxyl part of radicals being inaccessible to direct paramagnetic impacts. The constants of binding of paramagnetics to the membrane surface have been determined from these experiments. All results (including the assymetry of label rotation) can be explained most simply by assuming that the polar lipid groups are oriented parallel to the membranes surface.

Electron Spin Resonance Spectroscopy↗
PubMedDate not supplied

[Investigation of the microstructure of biological systems by triplet label].

A method for investigating the microstruct and dynamics of biological systems by means of triplet-excited molecules is suggested. The method is based on the phenomenon of triplet excitation disactivation by exchange-resonance triplet-triplet energy transfer to the acceptor or by intercombination conversion induced by interaction of an excited molecule with a paramagnetic center. The disactivation efficiency was measured by registrating the phosphorescense decay kinetics. The interaction of the triplet label eosin isothiocyanate, covalently coupled with albumine, lysozyme, sarcoplasmic reticulum membrane and Ca-Mg-dependent sarcoplasmic reticulum ATPase, with O2, the stable nitroxide radicals and ions of Mn2+ was investigated to analyse the potentialities of this method. As a model system the eosin phosphorescence quenching by the same quenchers in glycerine-aguaous solutions was studied. The method permits to investigate the microviscosity and microstructure of biological objects in the label attached region on interaction of the label with a sound-quencher with constants being 10(4) divided by 10(9) M-1 sec-1 and to measure the lateral diffusion of molecules in highly viscosity media (10 divided by 10(5) santypuas).

Adenosine Triphosphatases↗