Kamil Górecki
@kamil-gorecki.bsky.social
I’m deeply thankful to everyone at HuRibbe lab and UCIBioSci who made this project possible. It’s been an incredible journey, and I’m excited for what’s ahead.
May 30, 2025 at 12:27 AM
I’m deeply thankful to everyone at HuRibbe lab and UCIBioSci who made this project possible. It’s been an incredible journey, and I’m excited for what’s ahead.
From an evolutionary perspective, this supports the idea that a simpler nitrogenase once existed.
From a synthetic biology perspective, it’s a step toward artificial nitrogen fixers, and eventually, self-fertilizing plants.
By conscious design, not just by copying nature.
From a synthetic biology perspective, it’s a step toward artificial nitrogen fixers, and eventually, self-fertilizing plants.
By conscious design, not just by copying nature.
May 30, 2025 at 12:27 AM
From an evolutionary perspective, this supports the idea that a simpler nitrogenase once existed.
From a synthetic biology perspective, it’s a step toward artificial nitrogen fixers, and eventually, self-fertilizing plants.
By conscious design, not just by copying nature.
From a synthetic biology perspective, it’s a step toward artificial nitrogen fixers, and eventually, self-fertilizing plants.
By conscious design, not just by copying nature.
Therefore, we managed to simplify the set of genes and metabolites needed.
No molybdenum. No homocitrate. No specialized chaperones.
And we even connected it directly to E. coli’s native metabolism via an endogenous ferredoxin.
No molybdenum. No homocitrate. No specialized chaperones.
And we even connected it directly to E. coli’s native metabolism via an endogenous ferredoxin.
May 30, 2025 at 12:27 AM
Therefore, we managed to simplify the set of genes and metabolites needed.
No molybdenum. No homocitrate. No specialized chaperones.
And we even connected it directly to E. coli’s native metabolism via an endogenous ferredoxin.
No molybdenum. No homocitrate. No specialized chaperones.
And we even connected it directly to E. coli’s native metabolism via an endogenous ferredoxin.
Most previous efforts focused on copying the full gene cluster from natural nitrogen fixers. But the real goal isn’t to preserve every gene, it’s to enable nitrogen fixation in new hosts with just two things: an electron source and a catalyst that binds nitrogen.
May 30, 2025 at 12:27 AM
Most previous efforts focused on copying the full gene cluster from natural nitrogen fixers. But the real goal isn’t to preserve every gene, it’s to enable nitrogen fixation in new hosts with just two things: an electron source and a catalyst that binds nitrogen.
The answer is yes, as we demonstrate in our newest study. NifEN, paired with the Fe protein, can fix nitrogen in vivo in the model organism E. coli, which is normally incapable of nitrogen fixation.
May 30, 2025 at 12:27 AM
The answer is yes, as we demonstrate in our newest study. NifEN, paired with the Fe protein, can fix nitrogen in vivo in the model organism E. coli, which is normally incapable of nitrogen fixation.
I immediately recognized it as something more: a molecular fossil, a remnant of an ancestral nitrogenase that likely existed before the modern system emerged. And it reframed the problem: could we recreate a simpler, ancient nitrogenase system that still works in vivo?
May 30, 2025 at 12:27 AM
I immediately recognized it as something more: a molecular fossil, a remnant of an ancestral nitrogenase that likely existed before the modern system emerged. And it reframed the problem: could we recreate a simpler, ancient nitrogenase system that still works in vivo?
In our studies on nitrogenase, the nitrogen fixing enzyme, we made a surprising discovery last year. The maturase NifEN, long thought to merely assist in assembling nitrogenase, can reduce nitrogen on its own in vitro.
www.science.org/doi/10.1126/...
www.science.org/doi/10.1126/...
Cofactor maturase NifEN: A prototype ancient nitrogenase?
The nitrogenase cofactor maturase NifEN is capable of N2 reduction and may represent a prototype ancient nitrogenase.
www.science.org
May 30, 2025 at 12:27 AM
In our studies on nitrogenase, the nitrogen fixing enzyme, we made a surprising discovery last year. The maturase NifEN, long thought to merely assist in assembling nitrogenase, can reduce nitrogen on its own in vitro.
www.science.org/doi/10.1126/...
www.science.org/doi/10.1126/...
Yet nitrogen is all around us. If we could engineer self-fertilizing plants, it could transform agriculture. And there might already exist a blueprint.
May 30, 2025 at 12:27 AM
Yet nitrogen is all around us. If we could engineer self-fertilizing plants, it could transform agriculture. And there might already exist a blueprint.
Evolution may have already solved some of the biggest challenges we face today.
Take nitrogen fixation: essential for life, yet only a few microbes can do it. Most crops rely on synthetic fertilizers, which are costly and harmful to the environment.
Take nitrogen fixation: essential for life, yet only a few microbes can do it. Most crops rely on synthetic fertilizers, which are costly and harmful to the environment.
May 30, 2025 at 12:27 AM
Evolution may have already solved some of the biggest challenges we face today.
Take nitrogen fixation: essential for life, yet only a few microbes can do it. Most crops rely on synthetic fertilizers, which are costly and harmful to the environment.
Take nitrogen fixation: essential for life, yet only a few microbes can do it. Most crops rely on synthetic fertilizers, which are costly and harmful to the environment.
We recently published in Science Advances, a simplified nitrogenase system brought back to life in E. coli.
www.science.org/doi/full/10....
www.science.org/doi/full/10....
Heterologous synthesis of a simplified nitrogenase analog in Escherichia coli
Heterologous synthesis of a nitrogenase analog (NifH/NifEN) in E. coli enables N2 reduction and incorporation of N into biomass.
www.science.org
May 30, 2025 at 12:27 AM
We recently published in Science Advances, a simplified nitrogenase system brought back to life in E. coli.
www.science.org/doi/full/10....
www.science.org/doi/full/10....