Structural basis of biological nitrogen fixation
California Institute of Technology · Howard Hughes Medical Institute · +1 more institution
Abstract
Biological nitrogen fixation is mediated by the nitrogenase enzyme system that catalyses the ATP dependent reduction of atmospheric dinitrogen to ammonia. Nitrogenase consists of two component metalloproteins, the MoFe-protein with the FeMo-cofactor that provides the active site for substrate reduction, and the Fe-protein that couples ATP hydrolysis to electron transfer. An overview of the nitrogenase system is presented that emphasizes the structural organization of the proteins and associated metalloclusters that have the remarkable ability to catalyse nitrogen fixation under ambient conditions. Although the mechanism of ammonia formation by nitrogenase remains enigmatic, mechanistic inferences motivated by…
Citation impact
- FWCI
- 49.86
- Percentile
- 100%
- References
- 187
Authors
7- DCDouglas C. ReesCorresponding
California Institute of Technology, Howard Hughes Medical Institute
- FAF. Akif Tezcan
California Institute of Technology
- CHChad Haynes
California Institute of Technology
- MYMika Y. Walton
California Institute of Technology, Howard Hughes Medical Institute
- SLSusana L. A. Andrade
California Institute of Technology
Topics & keywords
- Nitrogenase
- Nitrogen fixation
- Electron transfer
- Chemistry
- Nitrogen
- Enzyme
- Cofactor
- Ammonia
- Clean water and sanitation