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Repression of nitrogenase by ethanol in nitrogen-deprived cultures of Rhodovulum sulfidophilum (1999)

Maeda, I ; Daba, M ; Hirose, N ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology letters 171 (1999), S. 0

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ISSN: 1574-6968

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Light-dependent H2 evolution did not occur in nitrogen-deprived cultures of Rhodovulum sulfidophilum in the presence of ethanol. When ethanol was added to cells which had been grown with ammonia, derepression of the nitrogen fixation genes (nifHD) was inhibited at an ethanol concentration of 1 mM. On the other hand, when cells had nitrogenase-catalyzed proton-reducing activity prior to ethanol addition, reduction of the nifHD transcript level did not occur after the addition. In cells grown with ammonia, concomitant addition of an auxiliary oxidant such as dimethylsulfoxide or sodium bicarbonate resulted in derepression of nitrogenase activity in the presence of ethanol. These results suggest that the electron-accepting process is necessary for derepression of nif genes in cultures which use ethanol as the electron donor.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6968.1999.tb13421.x

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Poly(3-hydroxybutyrate) as an endogeneous substrate for H 2 evolution in Rhodovulum sulfidophilum (1997)

Maeda, I. ; Idehara, K. ; Okayama, N. ; [et al.]

Springer

Biotechnology letters 19 (1997), S. 1209-1212

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ISSN: 1573-6776

Source: Springer Online Journal Archives 1860-2000

Topics: Process Engineering, Biotechnology, Nutrition Technology

Notes: Abstract In the absence of an external substrate, H 2 was evolved in Rhodovulum sulfidophilum under light-anaerobic conditions, along with degradation of poly(3-hydroxybutyrate) (PHB). Cells grown with succinate as a sole carbon source accumulated only a small amount of PHB compared with that in cells grown with a multiple substrate consisting of a mixture of four organic acids. Unlike PHB-containing cells, PHB-deficient cells did not evolve H in the absence of an external substrate. Nitrogenase activity was expressed while no hydrogenase activity was detected during the incubation of PHB-containing cells. These results suggest that intracellular PHB serves as a substrate for the H evolution catalyzed by nitrogenase when an external substrate is lacking.