Nitrogen fixation and hydrogen metabolism in photosynthetic bacteria

Meyer, Jacques; Kelley, Bruce C.; Vignais, Paulette M.

doi:10.1016/s0300-9084(78)80821-9

Cited by 91 publications

(51 citation statements)

References 89 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Difficulties in obtaining active nitrogenase in extracts of Rhodospirillum rubrum led to the discovery of a Mn2+-dependent activating factor for the enzyme (Ludden and Burris 1978). Similar results were described for Azospirillum lipoferum (Okon et al 1977; and Rhodopseudomonas species (Zumft and Castillo 1978;Meyer et al 1978). In Rhodospirillum and Rhodopseudomonas species, addition of NH4+, glutamate, or aspartate to N2-fixing cultures causes a reversible inactivation of the Fe protein (Zumft and Castillo 1978;Jones and Monty 1979;Meyer and Vignais 1979;Yoch 1979).…”

Section: Localization Of Nif Genessupporting

confidence: 75%

Progress in comparative genetics of nitrogen fixation

Robson¹,

Kennedy²,

Postgate³

1983

Can. J. Microbiol.

View full text Add to dashboard Cite

Section: Localization Of Nif Genessupporting

confidence: 75%

Progress in comparative genetics of nitrogen fixation

Robson¹,

Kennedy²,

Postgate³

1983

Can. J. Microbiol.

View full text Add to dashboard Cite

“…Protein concentrations were determined by using bicinchoninic acid reagent (Bio-Rad) with bovine serum albumin as a standard. For whole cells of R. capsulatus, proteins were estimated from the empirical relationship OD 660 /5 ϭ 1 mg of protein/ml (31). Native acrylamide gels were made like SDS-polyacrylamide gels, except that SDS and a concentration gel were omitted, and they were run in 0.5ϫ Laemmli buffer.…”

Section: Methodsmentioning

confidence: 99%

Interaction between the H ₂ Sensor HupUV and the Histidine Kinase HupT Controls HupSL HydrogenaseSynthesis in Rhodobactercapsulatus

2003

View full text Add to dashboard Cite

The photosynthetic bacterium Rhodobacter capsulatus contains two [NiFe]hydrogenases: an energy-generating hydrogenase, HupSL, and a regulatory hydrogenase, HupUV. The synthesis of HupSL is specifically activated by H 2 through a signal transduction cascade comprising three proteins: the H 2 -sensing HupUV protein, the histidine kinase HupT, and the transcriptional regulator HupR. Whereas a phosphotransfer between HupT and HupR was previously demonstrated, interaction between HupUV and HupT was only hypothesized based on in vivo analyses of mutant phenotypes. To visualize the in vitro interaction between HupUV and HupT proteins, a six-His (His 6 )-HupU fusion protein and the HupV protein were coproduced by using a homologous expression system. The two proteins copurified as a His 6 -HupUHupV complex present in dimeric and tetrameric forms, both of which had H 2 uptake activity. We demonstrated that HupT and HupUV interact and form stable complexes that could be separated on a native gel. Interaction was also monitored with surface plasmon resonance technology and was shown to be insensitive to salt concentration and pH changes, suggesting that the interactions involve hydrophobic residues. As expected, H 2 affects the interaction between HupUV and HupT, leading to a weakening of the interaction, which is independent of the phosphate status of HupT. Several forms of HupT were tested for their ability to interact with HupUV and to complement hupT mutants. Strong interaction with HupUV was obtained with the isolated PAS domain of HupT and with inactive HupT mutated in the phosphorylable histidine residue, but only the wild-type HupT protein was able to restore normal H 2 regulation.

show abstract

“…Though the primary role of nitrogenase is to provide fixed nitrogen, we find that this enzyme may also help cells with high rates of H 2 production dissipate excess electrons. Hydrogenase has been proposed to recycle H 2 in H 2 -producing cells (18). While we did find higher expression of hydrogenase-associated genes in H 2 -producing cells than in non-H 2 -producing cells ( Fig.…”

mentioning

confidence: 49%

Pathways Involved in Reductant Distribution during Photobiological H ₂ Production by Rhodobacter sphaeroides

Kontur

Ziegelhoffer

Spero

et al. 2011

Appl Environ Microbiol

View full text Add to dashboard Cite

show abstract

Nitrogen fixation and hydrogen metabolism in photosynthetic bacteria

Cited by 91 publications

References 89 publications

Progress in comparative genetics of nitrogen fixation

Progress in comparative genetics of nitrogen fixation

Interaction between the H ₂ Sensor HupUV and the Histidine Kinase HupT Controls HupSL HydrogenaseSynthesis in Rhodobactercapsulatus

Pathways Involved in Reductant Distribution during Photobiological H ₂ Production by Rhodobacter sphaeroides

Contact Info

Product

Resources

About

Nitrogen fixation and hydrogen metabolism in photosynthetic bacteria

Cited by 91 publications

References 89 publications

Progress in comparative genetics of nitrogen fixation

Progress in comparative genetics of nitrogen fixation

Interaction between the H 2 Sensor HupUV and the Histidine Kinase HupT Controls HupSL HydrogenaseSynthesis in Rhodobactercapsulatus

Pathways Involved in Reductant Distribution during Photobiological H 2 Production by Rhodobacter sphaeroides

Contact Info

Product

Resources

About

Interaction between the H ₂ Sensor HupUV and the Histidine Kinase HupT Controls HupSL HydrogenaseSynthesis in Rhodobactercapsulatus

Pathways Involved in Reductant Distribution during Photobiological H ₂ Production by Rhodobacter sphaeroides