In the presence of sufficient light and water the major limiting factor to plant growth is bioavailable nitrogen, ammonia. Nitrogen fixation in plants occurs under ambient conditions while industrial production of ammonia requires conditions so energy intensive they consume approximately 1% of the world's energy production annually. The iron-molybdenum cofactor (FeMoco) of the nitrogenase enzyme is the site of dinitrogen reduction to ammonia. The complex structure of the active site of nitrogenase comprises a bicapped trigonal prism of seven iron atoms, one molybdenum atom, and nine sulfur atoms. Recently, a high-resolution single crystal X-ray structure revealed an interstitial atom at the center of the cluster core which is most likely a nitrogen atom. Such a cluster was unprecedented in iron chemistry. Herein, a synthetic route to iron-nitride clusters with electronic structures similar to the cofactor of the nitrogenase is presented, and synthetic schemes utilizing these ferric-nitride clusters as scaffolds for the construction of a cluster similar to the cofactor are proposed. New synthetic methodologies relevant to synthetic analogues of the cofactor of nitrogenase are being developed.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Postdoctoral Individual National Research Service Award (F32)
Project #
1F32GM070170-01A1
Application #
6936718
Study Section
Special Emphasis Panel (ZRG1-F04A (20))
Program Officer
Lograsso, Philip
Project Start
2005-05-01
Project End
2007-04-30
Budget Start
2005-05-01
Budget End
2006-04-30
Support Year
1
Fiscal Year
2005
Total Cost
$43,976
Indirect Cost
Name
Harvard University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
082359691
City
Cambridge
State
MA
Country
United States
Zip Code
02138