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N Kurihara

Publications and source records attributed to N Kurihara.

At least 235 records · Page 13Linked to original sources
PubMed1982

ATP synthesis associated with the conversion of hexachlorocyclohexane related compounds.

Clostridium rectum strain S-17 converts gamma-1,2,3,4,5,6-hexachlorocyclohexane (HCH) related compounds to chlorobenzenes. The metabolites from gamma-1,2,3,4,5,6-hexachlorocyclohexene and gamma-1,3,4,5,6-pentachlorocyclohexene are identified as 1,2,4-trichlorobenzene and 1,4-dichlorobenzene, respectively. ATP synthesis, converting these chlorinated compounds, is observed in the cell suspension of C.rectum as indicated by luciferase-luciferin reaction and phosphorylation of 32P-labeled phosphate. These observation lead to the conclusion that HCH and related compounds serve as artificial electron acceptors of the Stickland reaction, and therefore, the reductive dechlorination is associated with ATP synthesis.

Adenosine Triphosphate↗
PubMed1980

Lindane degradation by cell-free extracts of Clostridium rectum.

For lindane degradation, a cell suspension of Clostridium rectum strain S-17 demands the addition of substrates such as leucine, alanine, pyruvate, a leucine-proline mixture, and molecular hydrogen. In the presence of leucine-proline mixture, lindane decomposed in parallel with isovaleric acid formation, and both lindane degradation and isovaleric acid formation were inhibited by monoiodoacetic acid, suggesting a close relation between lindane degradation and the Stickland reaction. Lindane was degraded by cell-free extracts of C. rectum in the presence of dithiothreitol (DTT). Radiogaschromatograms of n-hexane soluble metabolites from [14C] lindane showed the presence of monochlorobenzene and gamma-3,4,5,6-tetrachlorocyclohexene. Leucine, NADH, and NADPH were somewhat less active than DTT for lindane degradation in cell-free extracts. Reductive dechlorination seemed the major route of lindane degradation in cell-free extracts as well as in the intact cells of C. rectum.

Amino Acids↗
PubMed1980

L-Lysine: 2-oxoglutarate 6-aminotransferase. Subunit structure composed of non-identical polypeptides and pyridoxal 5'-phosphate-binding subunit.

L-Lysine:2-oxoglutarate 6-aminotransferase from Flavobacterium lutescence (= Achromobacter liquidum) has been shown to be composed of one each of four non-identical subunits, A, B1, B2, and C. The subunits were isolated by gel filtration, and DEAE-cellulose chromatography in the presence of 8 M urea. Their molecular weights were determined by ultracentrifugation, gel electrophoresis and gel filtration: subunit A 24,000; B1 28,000; B2 28,000; C 45,000. These subunits were all different in amino acid composition. Of the two molecules of bound pyridoxal 5'-phosphate, the one which absorbs at 415 nm is bound to subunit B2 and participates in the catalytic action of the enzyme.

Amino Acids↗