• Microbiology and Biotechnology Letters
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• v.13 no.3
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• pp.257-263
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• 1985

Rhodopseudomonas sp. KCTC 1437 evolved molecular hydrogen efficiently under light illuminated anaerobic culture condition in the presence of organic acids and various sugars. especially glucose when low concentration of NH$_4$ + or L-glutamate was added to cultures. It was revealed that hydrogen formation from Rhodopseudomonas sp. KCTC 1437 was mediated by two different enzyme systems. Under the nitrogen limiting condition, hydrogen evolution from glucose was catalyzed by nitrogenase. For the nitrogenase activation in vivo, the precultured cells drown on limiting concentration of NH$_4$$^{+}$ as a sole nitrogen source showed more capacity of hydrogen evolution from glucose in the presence of L-glutamate than any other cells .frown on sufficient concentration of NH$_4$$^{+}$, L-glutamate, NH$_4$$^{+}$, or both of L-glutamate and $N_2$. A significant volume of molecular hydrogen was evolved from glucose even in the presence of excess NH$_4$$^{+}$ either in the light or dark anaerobic condition, presumably due to the mediation of hydrogen evolution by fromic hydrogenlyase.enlyase.

• Korean Journal of Microbiology
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• v.28 no.2
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• pp.151-157
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• 1990

The maximum nitrogen fixation activity of the associative, microaerobic and acid tolerant bacteria, Azospirillum amazonense Kp1 was obtained with 0.2Kpa of $O_{2}$ and showed a reversible inhibition by the higher concentrations. Ammonium treatment caused a gradual inhibition of the activity up to 350mM. The nitrogenase systems were purified by gradient chromatography on DEAE-52 cellulose, heat treatment and preparative PAGE. The MoFe protein showed molecular weight of 210,000 including two nonidentical subunits with apparent molecular weights of 55,000 and 50,000 and an isoelectricpoint of 5.2 and contained 2, 24 and 28 atoms of Mo, Fe and acid labile S per molecule. The Fe protein revealed molecular weight of 66,000 including two types of subunits with molecular weights of 35,000 and 31,000 and an isoelectric point of 4.6, and contained 4 atoms of Fe and 6 atoms of S per molecule. The maximum specific nitrogenase activity attained 2,200 and 1,700nM $C_2H_4mg^{-1} min^{-1}$, respectively for MoFe and Fe proteins at pH7 and $35^{\circ}C$. The activity was lost after 10 and 30 days under the cold room ($4^{\circ}C$) condition for Fe and MoFe proteins, respectively.

• Korean Journal of Soil Science and Fertilizer
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• v.17 no.4
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• pp.415-427
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• 1984

This experiment was carried out to investigate the distribution of associative nitrogen fixers, Azospirillum spp. and their nitrogenase activities measured by ARA in the rhizosphers of rice, soybean, and weed grown in the rice paddy field at ear formation stage of rice. Nitrogenase activities produced by Azospirillum spp. enriched from histophere ranged from 16 to 53 n mole/tube/hr.. High nitrogen fixing activities more than 30 n mole/tube/hr. were observed in the histophere of the Echinochloa crus-galli L., Finbristylis miliacea L., and Monochoria vaginalis var.. Nitrogen fixing activities of Azospirillum spp. obtained from single colonies which originated from the rhizoplane of rice (pot-kwang var.), Finbris tylis miliacea L., Monochoria vaginaliz var., Glycine max L. were higher over 100 n mole/tube/hr. than those histophere. Genus of Azopsirillum isoltated from roots of the Graminease (Oriza sativa L., $C_3$-plant, Echinochloa crus=galli L., $C_4$-plant, Cyperus difforuis L.. $C_4$-plant), and Aeschynomene indica L. (Leguminosae, $C_3$-plant) was identified as A. brasilense. However, both strains, A. lipoferum and A. brasilense ($nir^-$ or $nir^+$ strain) were isolated from other plant roots, Both $nir^-$ and $nir^+$ strains of A. brasilense were associated with the same host plant.