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L N Matveeva

Publications and source records attributed to L N Matveeva.

14 recordsLinked to original sources

The missing organic molecules on Mars.

GC-MS on the Viking 1976 Mars missions did not detect organic molecules on the Martian surface, even those expected from meteorite bombardment. This result suggested that the Martian regolith might hold a potent oxidant that converts all organic molecules to carbon dioxide rapidly relative to the rate at which they arrive. This conclusion is influencing the design of Mars missions. We reexamine this conclusion in light of what is known about the oxidation of organic compounds generally and the nature of organics likely to come to Mars via meteorite. We conclude that nonvolatile salts of benzenecarboxylic acids, and perhaps oxalic and acetic acid, should be metastable intermediates of meteoritic organics under oxidizing conditions. Salts of these organic acids would have been largely invisible to GC-MS. Experiments show that one of these, benzenehexacarboxylic acid (mellitic acid), is generated by oxidation of organic matter known to come to Mars, is rather stable to further oxidation, and would not have been easily detected by the Viking experiments. Approximately 2 kg of meteorite-derived mellitic acid may have been generated per m(2) of Martian surface over 3 billion years. How much remains depends on decomposition rates under Martian conditions. As available data do not require that the surface of Mars be very strongly oxidizing, some organic molecules might be found near the surface of Mars, perhaps in amounts sufficient to be a resource. Missions should seek these and recognize that these complicate the search for organics from entirely hypothetical Martian life.

Alkanes↗

[The nature of phosphate residue binding in the phosphorylated form of succinyl-CoA-synthetase from pigeon breast muscle].

The hydrolytic stability of phosphorylated pigeon breast muscle succinyl-CoA synthetase within a wide pH range was studied. It was found that within complex I the phosphate-protein bond is hydrolyzed at alkaline values of pH (11.0 and 13.0); at acidic pH values this bond is hydrolyzed by 50%. Within complex II the phosphate-protein bond is hydrolyzed at acidic pH values and is stable at alkaline pH values. The reaction of the phosphorylated enzyme with hydroxylamine and diisopropylfluorophosphate results in protein dephosphorylation by 50%. Ion-exchange chromatography of the radioactive phosphorylated enzyme II alkaline hydrolyzate (3 n NaOH, 3 hours, 100 degrees C) revealed that the radioactivity was distributed between 1-N-, 3-N-phosphohistidine and 1.3-N-diphosphohistidine fractions. The experimental results suggest that in the phosphorylated enzyme I phosphate is bound to the protein to form an acyl phosphate and phosphoester bonds, while in the phosphorylated enzyme II phosphate binding to the protein occurs with the formation of phosphoamide bonds.

Animals↗

[Reaction mechanism of succinyl CoA synthetase from pigeon thoracic muscle].

The ability of succinyl-CoA-synthetase from pigeon thoracic muscle to interact with ATP is investigated. gamma-32P-ATP and 8-14C-ATP were used in experiments. It is found that the enzyme, when reacting with ATP in the presence of Mg2+, forms a complex containing 2 moles of ATP residue and 2 moles of phosphoric acid residue (splitted from ATP) per 1 mole of protein. After 2 hours of incubation at 0-4 degrees C, the complex is converted into another one, containing 4 residues of phosphoric acid per 1 mole of @protein. Both complexes are active, and their incubation with succinate and CoA results in the formation of succinyl-CoA. The reaction capacity of these enzyme complexes with some reaction substrates is investigated. The enzyme complex containing 2 phosphoric acid residues and 2 nucleotide residues is found to interact neither with CoA, nor with succinate. The enzyme complex containing 4 phosphoric acid residues does not react with CoA, but it interacts with 14C-succinate, releasing inorganic phosphate in the amount equivalent to the equimolar amount of protein-binding succinic acid.

Adenosine Triphosphate↗

[Degradation of polycyclic aromatic hydrocarbons by a strain of Pseudomonas fluorescens 16N2].

The growth of Pseudomonas fluorescens 16N2 on naphthalene was accompanied with accumulation of salicylate in the culture medium and induction of gentisate 1,2-dioxygenase and catechol 1,2-dioxygenase. The transformation of anthracene by the cells growing on hexadecane led to the formation of 3-hydroxy-2-naphthoate and salicylate. Pathways for naphthalene and anthracene degradation are proposed.

Biodegradation, Environmental↗

[Mechanism of the reaction of substrate phosphorylation in the tricarboxylic acid cycle].

The suggested sequence of the reactions differs from those presented in literature and includes the following compounds as intermediate ones: the complex of enzyme having 2ATP and two residues of phosphoric acid; the complex of enzyme having four residues of phosphoric acid; the complex of enzyme containing two residues of phosphoric acid and two residues of succinic acid. Sequences of the reactions suggested in literature involve as intermediate compounds a phosphorylated derivative of the enzyme (E--P), phosphorylated derivative CoA linked with the enzyme (E.CoA--P), a high-ergic compound of the enzyme with CoA (E.CoA) and succinyl phosphate linked with the enzyme (E.succinyl--P).

Adenosine Triphosphate↗

[Tn5-mutagenesis of the styrene-degrading strain Pseudomonas sp. Y2. Analysis of transformation products and DNA-scopy of the mutants obtained].

The bacterium Pseudomonas sp. Y2 using styrene as a sole source of carbon and energy was subjected to transposon Tn5(Kmr) mutagenesis. The mutants were divided into three classes by the ability to grow on styrene, 2-phenylethanol, and phenylacetate. It is shown that 2-phenylethanol is not an obligate metabolite of styrene transformation. This allows the conclusion that in Pseudomonas sp. Y2 styrene can be degraded via consistent oxidation of the side chain by two pathways. For the comparison of strains/mutants and determination of genetic markers, DNA-fingerprinting of total DNA was carried out using electrophoresis of restriction fragments and blot-hybridization with different 32P-DNA-probes.

Biodegradation, Environmental↗