Open AccessJournal Article
Nitrogen fixation hundred years after
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About: This article is published in Research in Microbiology. The article was published on 01 Jan 1988. and is currently open access. The article focuses on the topics: Nitrogen fixation.
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Citations
Effect of temperature on flavonoid production in pigeonpea [Cajanus cajan (L) Millsp] in relation to nodulation
TL;DR: At the higher temperature the flavonoids exuded from pigeonpea roots were same those in the root homogenate, and the proportion of the second flavonoid in the pigepea and the mungbean was higher and theportion of the third flavonoidal was lower at 37°C compared to 30°C.
17
Identification of sulfurtransferase enzymes in Azotobacter vinelandii.
TL;DR: Rhodanese and 3‐mercaptopyruvate sulphurtransferase have been identified in A. vinelandii and two distinct active fractions of the two sulphur transferases were obtained after FPLC ion‐exchange chromatography of material partially purified from crude extracts.
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Control of nitrogenase in Azospirillum sp.
TL;DR: The DRAT and DRAG system does not appear to function in Acetobacter diazotrophicus, an organism isolated from sugar cane, that fixes N2 at a pH as low as 3.0 and does show a rather sluggish response to NH4 +.
16
Whole cell hybridization as a tool to study Frankia populations in root nodules
TL;DR: The analysis of uncultured Frankia populations in root nodules can reliably be performed on a subgroup level when digoxigenin-labeled oligonucleotide probes or in vitro transcripts directed against an actinomycetes-specific insertion on the 23S rRNA are used.
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References
Metabolic pathways in Paracoccus denitrificans and closely related bacteria in relation to the phylogeny of prokaryotes.
TL;DR: It is concluded that pathway specificc-type cytochromes are involved in denitrification and methylotrophy in Paracoccus denitrificans and the distribution of complex metabolic systems in eubacteria and in a number of species belonging to the α-group of purple non sulphur bacteria is reviewed.
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In vitro synthesis of the iron-molybdenum cofactor of nitrogenase. Purification and characterization of NifB cofactor, the product of NIFB protein.
TL;DR: NifB-co has been purified to homogeneity by a unique one-step method and is stable to repeated freeze-thaw cycles and is also stable in N-methylformamide, the solvent used for the isolation of FeMo-co.