I am excited to share that my first research paper is now available online at @mBio: We explore the role of #ferredoxins (Fds) in nitrogen (N2) fixation by #nitrogenases (N2ases), the only enzymes to convert atmospheric N2 into bioavailable ammonia (NH3).

RT @ChemEurJ: Leveraging spectroscopic & structural approaches - @HollyGAddison, @AJPierik, @RebeleinLab & team obtained new insights into….

RT @RebeleinLab: Using spectroscopic and structural approaches we gained new insights into the role of #ferredoxins in N2 fixation. Just pu….

RT @AJPierik: Dear nitrogenase lovers: have a look at our BioRxiv prepublication. Ana Maciel, Jessica Soares, . , Antonio Pierik and Johan….

Apologies there was a typo, journal is @mbiojournal.

@mbio I would like to thank the co-authors on this publication, Dr. Timo Glatter and @KaHochberg. Also, a special thanks to my PhD supervisor @RebeleinLab!.

@mbio Both Fds are excellent targets for bioengineering the e- flux to the Fe-N2ase with aims to further increase the conversion of N2to NH3.

@mbio We found that 2 distinct Fds with different redox centres are essential for N2-fixation by the Fe-N2ase, though surprisingly, our results suggest the 2 Fds likely have separate roles in N2-fixation.

@mbio We investigate the unknown e- transfer to the Fe-N2ase and tackle the question whether Fds are specific or redundant in the e- transport to the Fe-N2ase in Rhodobacter capsulatus.

RT @DSchindler_PDR: Happy to see our Nanopore sequencing workflow for construct validation published. Congratulations @adanramirezro, @CedK….

Finally, I would like to thank the co-authors on this publication, Dr. Timo Glatter and @KaHochberg. Also, a special thanks to my PhD supervisor @RebeleinLab. Thanks for reading 😀.

In conclusion, we established that 2 distinct Fds with different redox centres are essential for Fe-N2ase mediated N2-fixation. These Fds are excellent targets for bioengineering aiming to further increase the conversion of N2 to NH3and CO2 to hydrocarbons by the Fe-N2ase.

The distinct growth and activity behaviour upon re-introduction of FdN compared to FdC suggested these Fds likely have different roles. This was corroborated by differences in the production of N2-fixation associated proteins in the FdN or FdC deletion strains:

To recover the deletion strains, we introduced fdxN and fdxC on plasmids. Multiple or single copies of fdxNrecovered cells to WT growth and activity levels. For fdxC, a single copy partially recovered WT behaviour while introducing multiple copies was lethal to cells:

We then deleted the genes for each N2-fixation relevant Fd in R. capsulatus and observed that deletion of only 2 Fds, FdN and FdC, impacted N2-fixation shown through slower growth on N2 and less N2ase activity for the reduction of acetylene:

We study R. capsulatus, a fascinating N2-fixing bug, which has 6 distinct Fds. We discovered through proteome analysis that only 4 of these Fds are over-produced under N2-fixing conditions, meaning they likely have roles in Fe-N2ase mediated N2-fixation.

Here we investigate the unknown e- transfer to the Fe-N2ase and tackle the question whether Fds are specific or redundant in the e- transport to the Fe-N2ase in Rhodobacter capsulatus (R. capsulatus).

Fds are redox proteins, either donating electrons (e-) or accepting e-. Fds are known to drive N2ases by donating low potential e- for the splitting of N2.

Our manuscript is now online @Bioarchivepreprint! We explore the role of #ferredoxins (Fds) in nitrogen (N2) fixation via #nitrogenases (N2ases), the only enzymes to convert atmospheric N2 into bioavailable ammonia (NH3) and CO2 directly to hydrocarbons.

RT @RebeleinLab: Great talk by @HollyGAddison about the electron transport to the iron #nitrogenase by #ferredoxins #VAAM2023 https://t.co/….