Nitrogenases are essential enzymes that play a crucial role in the geochemical processes on our planet. These enzymes are responsible for converting gaseous nitrogen into bioavailable ammonia, which is a fundamental building block for all forms of life. However, recent research by a team of scientists in Marburg, Germany, led by Johannes Rebelein, has shed light on the previously unknown ability of some nitrogenases to also convert CO2 into valuable hydrocarbon chains. This discovery has opened up new possibilities for the development of biotechnological processes that could revolutionize sustainable bioproduction.
The team of researchers focused on investigating the substrate specificity and preferences of nitrogenase enzymes. Through their experiments, they challenged the conventional understanding of nitrogenases and highlighted their potential for sustainable bioproduction. The results of their study, published in the journal Science Advances, revealed that certain nitrogenases have the ability to efficiently reduce CO2 to produce hydrocarbons such as methane, ethylene, ethane, and formic acid. These products are not only valuable as potential energy sources but also as industrially important chemicals.
Insights from the Study
The researchers conducted their experiments on the photosynthetic bacterium Rhodobacter capsulatus, which possesses two different types of nitrogenase enzymes: the molybdenum (Mo) nitrogenase and the iron (Fe) nitrogenase. Their findings showed that the Fe nitrogenase is three times more efficient at reducing CO2 than the Mo nitrogenase. Moreover, when both enzymes were exposed to CO2 and N2 simultaneously, the Fe nitrogenase displayed a preference for CO2 as a substrate, while the Mo nitrogenase selectively reduced N2. This surprising result challenges the traditional view of nitrogenases as solely nitrogen-converting enzymes and opens up new avenues for the development of novel CO2 reductases.
One of the most intriguing discoveries from the study was the observation that the Fe nitrogenase-catalyzed CO2 reduction process could occur even in the absence of additional CO2 in the culture medium. This finding suggests that the microbial communities that harbor nitrogenase enzymes may have a broader impact on their environment than previously thought. Additionally, the ability of photosynthetic bacteria like R. capsulatus to use light energy to stimulate nitrogenases for CO2 conversion indicates a potential shift towards a sustainable circular economy. The energy captured from sunlight by these bacteria could be stored in the hydrocarbons produced by nitrogenase, offering a promising avenue for sustainable bioproduction.
The research led by Johannes Rebelein and his team has provided valuable insights into the untapped potential of nitrogenase enzymes for sustainable bioproduction. By challenging the current understanding of nitrogenases and highlighting their versatility in converting CO2 into valuable products, the study paves the way for the development of innovative biotechnological processes. The findings not only have implications for the biotechnology industry but also for our broader societal goals of achieving a sustainable and circular economy.Nitrogenases are among the most geochemically important enzymes on Earth, providing all forms of life with bioavailable nitrogen in the form of ammonia (NH3). Some nitrogenases can also directly convert CO2 into hydrocarbon chains, making them an exciting target for the development of biotechnological processes. A team of researchers in Marburg, Germany, led by Max Planck scientist Johannes Rebelein, has now provided a comprehensive insight into the substrate specificity and preferences of nitrogenase. Their results challenge the current understanding of nitrogenases and highlight their potential for sustainable bioproduction. The research is published in the journal Science Advances. Nitrogen is one of the main building blocks of our cells. However, most of the nitrogen on Earth occurs as gaseous N2 and is chemically unusable by cells. Only a single family of enzymes is able to convert N2 into the bioavailable form of ammonia (NH3): nitrogenases. Researchers led by Johannes Rebelein from the Max Planck Institute for Terrestrial Microbiology in Marburg have discovered that some nitrogenases can also deal with another important substrate: They reduce the greenhouse gas CO2 to hydrocarbons (methane, ethylene, ethane) and formic acid. All these products are potential energy sources and industrially important chemicals. With a view to sustainable, carbon-neutral bioproduction, the team wanted to know: How well can the enzymes discriminate between CO2 and N2? And do microorganisms that grow on N2 also reduce CO2 under normal, physiological conditions?To answer these questions, the researchers focused on the photosynthetic bacterium Rhodobacter capsulatus, which harbors two isoenzymes: the molybdenum (Mo) nitrogenase and the iron (Fe) nitrogenase, which the bacterium needs as a reserve in the event of molybdenum deficiency. The researchers isolated both nitrogenases and compared their CO2 reduction using biochemical tests. They found that the Fe nitrogenase actually reduces CO2 three times more efficiently than its molybdenum containing counterpart and produces formic acid and methane at atmospheric CO2 concentrations. When both enzymes were offered CO2 and N2 at the same time, another important difference became apparent: while Mo-nitrogenase selectively reduces N2, Fe-nitrogenase tends to choose CO2 as a substrate. “Normally, a higher reaction speed in enzymes comes at the expense of accuracy. Interestingly, Mo-nitrogenase is both faster and more selective, showing its advantage in N2 reduction. The lower specificity of Fe nitrogenase and its preference for CO2 make it a promising starting point for the development of novel CO2 reductases,” says Frederik Schmidt, Ph.D. student in Johannes Rebelein’s lab and co-author of the study. The low selectivity was not the only surprise. “We analyzed which fraction of electrons ended up in which product and found that methane and high concentrations of formic acid derived from CO2 conversion by Fe nitrogenase were secreted by the bacteria even when no additional CO2 was added to the culture: the metabolically derived CO2 was sufficient to drive this process. This finding suggests that Fe nitrogenase-catalyzed CO2 reduction may indeed be widespread in nature,” says Niels Oehlmann, co-first author of the study. This also means that the availability and exchange of one-carbon substrates is likely to influence microbial communities in different environments. The work challenges the traditional view of nitrogenases as true nitrogen-converting enzymes. Photosynthetic bacteria such as R. capsulatus, which use light energy to stimulate nitrogenases to convert the greenhouse gas CO2, could play a key role not only in their environmental impact, but also in the societal shift towards a sustainable circular economy, says Johannes Rebelein. “The idea is that we can store the energy from the sunlight captured by the microorganism’s photosynthetic apparatus in the hydrocarbons produced by nitrogenase.
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