Predicting compatibility between ferredoxins and the Fe protein of nitrogenase using in silico protein modeling https://www.biorxiv.org/content/10.1101/2025.08.21.671581v1
August 22, 2025 at 3:17 AM
Predicting compatibility between ferredoxins and the Fe protein of nitrogenase using in silico protein modeling https://www.biorxiv.org/content/10.1101/2025.08.21.671581v1
Predicting compatibility between ferredoxins and the Fe protein of nitrogenase using in silico protein modeling https://www.biorxiv.org/content/10.1101/2025.08.21.671581v1
August 22, 2025 at 3:17 AM
Predicting compatibility between ferredoxins and the Fe protein of nitrogenase using in silico protein modeling https://www.biorxiv.org/content/10.1101/2025.08.21.671581v1
In a heroical effort, Yiting She produced and screened 13 different ferredoxins, identifing the truncated protein from Micractinium conductrix (McFdtr) as most competent for H2 production.
Notably, no significant extra driving force was neccessary, which renders McFdtr a "micro hydrogenase" 💪🏻
Notably, no significant extra driving force was neccessary, which renders McFdtr a "micro hydrogenase" 💪🏻
June 26, 2025 at 11:50 AM
In a heroical effort, Yiting She produced and screened 13 different ferredoxins, identifing the truncated protein from Micractinium conductrix (McFdtr) as most competent for H2 production.
Notably, no significant extra driving force was neccessary, which renders McFdtr a "micro hydrogenase" 💪🏻
Notably, no significant extra driving force was neccessary, which renders McFdtr a "micro hydrogenase" 💪🏻
Leveraging spectroscopic and structural approaches we obtained new insights into the role of #ferredoxins in N2 fixation. Just published in Chemistry – A European Journal: doi.org/10.1002/chem...! Great work by Holly Addison. Fantastic collaboration with Antonio Pierik on the EPR characterization.
Two Key Ferredoxins for Nitrogen Fixation Have Different Specificities and Biophysical Properties
Two ferredoxins, FdC and FdN, are collectively essential for the process of nitrogen fixation by the iron nitrogenase in R. capsulatus. We explore the biophysical factors, through spectroscopic and s....
doi.org
June 1, 2025 at 9:46 AM
Leveraging spectroscopic and structural approaches we obtained new insights into the role of #ferredoxins in N2 fixation. Just published in Chemistry – A European Journal: doi.org/10.1002/chem...! Great work by Holly Addison. Fantastic collaboration with Antonio Pierik on the EPR characterization.
It was a lot of fun to have @dstrenkert.bsky.social from @msudoeplantlab.bsky.social visit us and present her research on Ferredoxins last week 🥰 @carnegiescience.bsky.social
May 28, 2025 at 12:07 AM
It was a lot of fun to have @dstrenkert.bsky.social from @msudoeplantlab.bsky.social visit us and present her research on Ferredoxins last week 🥰 @carnegiescience.bsky.social
Ross @milton-group.bsky.social came up with a very similar idea: how about introducing cyanophenylalanine to a (bacterial) ferredoxin that binds two [4Fe-4S] clusters?
One might learn where the electron resides as most ferredoxins are considered one-electron redox mediators... 🧵
One might learn where the electron resides as most ferredoxins are considered one-electron redox mediators... 🧵
First off, let me highlight recent work from Vincent et al.: the authors modified plant ferredoxin with cyanophenylalanine and succeeded in measuring FeS-redox-dependent nitrile band shifts in the IR spectra.
May 21, 2025 at 6:59 PM
Ross @milton-group.bsky.social came up with a very similar idea: how about introducing cyanophenylalanine to a (bacterial) ferredoxin that binds two [4Fe-4S] clusters?
One might learn where the electron resides as most ferredoxins are considered one-electron redox mediators... 🧵
One might learn where the electron resides as most ferredoxins are considered one-electron redox mediators... 🧵
New Article: "Ferredoxin-mediated mechanism for efficient nitrogen utilization in maize" rdcu.be/ecus2
...based on the balance of nitrate-sensitive interaction between ferredoxins Fd4 and Fd9, antagonistically targeting NiR enzymes, thus regulating NO3– assimilation. #PlantScience
...based on the balance of nitrate-sensitive interaction between ferredoxins Fd4 and Fd9, antagonistically targeting NiR enzymes, thus regulating NO3– assimilation. #PlantScience
March 6, 2025 at 7:47 PM
New Article: "Ferredoxin-mediated mechanism for efficient nitrogen utilization in maize" rdcu.be/ecus2
...based on the balance of nitrate-sensitive interaction between ferredoxins Fd4 and Fd9, antagonistically targeting NiR enzymes, thus regulating NO3– assimilation. #PlantScience
...based on the balance of nitrate-sensitive interaction between ferredoxins Fd4 and Fd9, antagonistically targeting NiR enzymes, thus regulating NO3– assimilation. #PlantScience
Two distinct ferredoxins are essential for nitrogen fixation by the iron nitrogenase in Rhodobacter capsulatus https://www.biorxiv.org/content/10.1101/2023.12.07.570605v1
Two distinct ferredoxins are essential for nitrogen fixation by the iron nitrogenase in Rhodobacter capsulatus https://www.biorxiv.org/content/10.1101/2023.12.07.570605v1
Nitrogenases are the only enzymes able to fix gaseous nitrogen into bioavailable ammonia and, hence,
www.biorxiv.org
December 8, 2023 at 2:47 AM
Two distinct ferredoxins are essential for nitrogen fixation by the iron nitrogenase in Rhodobacter capsulatus https://www.biorxiv.org/content/10.1101/2023.12.07.570605v1
Two distinct ferredoxins are essential for nitrogen fixation by the iron nitrogenase in Rhodobacter capsulatus https://www.biorxiv.org/content/10.1101/2023.12.07.570605v1
Two distinct ferredoxins are essential for nitrogen fixation by the iron nitrogenase in Rhodobacter capsulatus https://www.biorxiv.org/content/10.1101/2023.12.07.570605v1
Nitrogenases are the only enzymes able to fix gaseous nitrogen into bioavailable ammonia and, hence,
www.biorxiv.org
December 8, 2023 at 2:47 AM
Two distinct ferredoxins are essential for nitrogen fixation by the iron nitrogenase in Rhodobacter capsulatus https://www.biorxiv.org/content/10.1101/2023.12.07.570605v1