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Published December 1993 | public
Journal Article

Dinitrogen Reduction by Nitrogenase: If N_2 Isn't Broken, It Can't be Fixed

Abstract

Nitrogenase consists of two component metalloproteins, the iron protein and molybdenum-iron protein, which together catalyze the ATP-dependent reduction of dinitrogen to ammonia during biological nitrogen fixation. With the recent crystal structure determinations of both proteins, a structural framework is now available for interpreting the mechanism of nitrogenase at the molecular level.

Additional Information

© 1993 Current Biology Ltd. This work was supported by National Institutes of Health grant GM45162 and National Science Foundation grant DMB91-18689. The contributions of J. Kim, MM Georgiadis, BT Hsu, H Komiya, MK Chan, D Woo, JL Schlessman, MW Day, AJ Chirino, MHB Stowell and L Joshua-Tor to the crystallographic work at Caltech, along with most enjoyable discussions with JB Howard, made this review possible.

Additional details

Created:
August 20, 2023
Modified:
October 20, 2023