Christine Morrison, University of California, San Diego
Nitrogenase has captured the minds of scientists for decades, as it contains two unique iron-sulfur clusters and is the only enzyme capable of reducing nitrogen to ammonia. Industrially, nitrogen fixation is accomplished using the Haber-Bosch process, and we are dependent on it to produce enough fertilizer to feed the world’s ever-increasing population. While the importance of the Haber-Bosch process cannot be overstated, several drawbacks exist such as high natural gas consumption and nitrate runoffs from excess fertilizer. These could be mitigated by learning and applying how nitrogenase forms and operates under ambient conditions. My work contributes to our understanding of biological nitrogen fixation through biophysical characterization of nitrogenase, including identification of the central atom in the “FeMo-cofactor” at the heart of nitrogenase, substrate pathways, and a protonated resting state. As we continue to learn more about nitrogenase, we may one day elucidate the enigmatic mechanism of biological nitrogen fixation. This knowledge could contribute to the development of more efficient nitrogen-fixing catalysts for industrial fertilizer synthesis or the design of de novo nitrogen-fixing proteins that could be expressed in plants so crops could essentially fertilize themselves.
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