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Previously, it has been impossible to capture the high-resolution images of nitrogenase, the only enzyme capable of reducing nitrogen into ammonia, during catalytic action. Now, for the first time, researchers at the University of California San Diego report near-atomic-resolution snapshots of nitrogenase during catalysis using cryogenic electron microscopy (cryoEM). The results were published in the journal Science.

This work was accomplished through a close partnership between the groups of Professor Akif Tezcan and Assistant Professor Mark Herzik, both in UC San Diego's Department of Chemistry and Biochemistry. While Tezcan has long studied nitrogenase, Herzik provided the cryoEM expertise needed to carry out the research.

"This is a very important advance in terms of biological nitrogen fixation as well as structural biology, in general," stated Tezcan. "To be able to obtain atomic-level-resolution pictures of an enzyme as dynamic and complex as nitrogenase in action is extremely exciting. It opens the doors to fully understanding the mechanism of this enigmatic enzyme, which has preoccupied researchers for decades."

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