Welcome to the new version of CaltechAUTHORS. Login is currently restricted to library staff. If you notice any issues, please email coda@library.caltech.edu
Published January 2015 | metadata_only
Journal Article

The Center of Biological Nitrogen Fixation: FeMo-Cofactor


The enzyme nitrogenase is the only known biological system capable of reducing atmospheric dinitrogen to ammonia, and is therefore an essential player in the biological nitrogen cycle. Despite decades of research, essential questions about the mechanism of nitrogen fixation are unanswered. The complexity of the nitrogenase active site FeMo-cofactor contributes thereby significantly to the problems nitrogenase research is facing today. Attempts to mimic its exceptional catalytic properties were without success and also the metal center itself exposed only a small fraction of its secrets so far. Today, the FeMo-cofactor is still the largest and most complex metal center known in biological systems. Solely its structure determination turned out to be an unexpected long process facing multiple hurdles. Even though X-ray crystallography led to first structural data of the [7Fe:9S:C:Mo]:R-homocitrate entity more than twenty years ago, only recently the entire atomic structure of the metal center was revealed. This review gives a short overview of the FeMo-cofactor with a special focus on its structure determination.

Additional Information

© 2014 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Received: April 8, 2014. Article first published online: 5 Aug. 2014. I thank Oliver Einsle, Douglas C. Rees, Erik Schleicher, Stefan Weber, Limei Zhang, Kathryn Perez, Eva Burger, Daniel Sippel, Julia Schlesier and Katerina Dörner for their support as well as stimulating discussions. The work was supported by the Deutsche Forschungsgemeinschaft and the European Research Council. Special Issue: Reactive Nitrogen-Containing Species: Generation, Characterization and Functionalization

Additional details

August 22, 2023
August 22, 2023