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Revealing the Molecular Underpinnings of a Key Enzyme
Published: November 30, 2010
Posted: March 26, 2013

As a major component of the biological nitrogen cycle, the bacterial enzyme nitrogenase (N2ase) converts nitrogenfrom air into ammonia, thereby making it accessible to plant life. The enzyme achieves this feat at a metal-sulfur cluster called the FeMo cofactor by a mechanism that still is not wellunderstood. Research to better understand how metals and metal clusters interact with nitrogen and reduced nitrogen species is exploiting the soft X-ray region via transition metal L-edgeand nitrogen K-edge spectroscopy. Complementary studies haveused the stopped-flow infrared system in the mezzanine spectroscopysuite at the Advanced Light Source at Lawrence Berkeley National Laboratory to probe time-dependent binding of the carbon monoxide molecule CO to N2ase.

Reference: Yang, Z.-Y., et al. 2011. “Steric Control of the Hi-CO MoFe Nitrogenase Complex Revealed by Stopped-Flow Infrared Spectroscopy,” Angewandte Chemie International Edition 50, 272–75. (Reference link)

Contact: Roland F. Hirsch, SC-23.2, (301) 903-9009
Topic Areas:

  • Research Area: Microbes and Communities
  • Research Area: Structural Biology, Biomolecular Characterization and Imaging
  • Research Area: Structural Biology Infrastructure

Division: SC-33.2 Biological Systems Science Division, BER

 

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