Electron Transfer of Nitrogenase Complex
EMSL Project ID
51747
Abstract
We propose to use EMSL supercomputing resources to gain a molecular level understanding of the mechanism of the Azotobacter vinelandii Mo-nitrogenase complex (N2ase), the key enzyme for nitrogen reduction to ammonia. Specially, we aim at elucidating the structural and dynamical regulation of the kinetics of the electron transfer to the catalytic cofactor. The project is intimately related to the DOE Basic Energy Sciences Physical Biosciences programs at PNNL (PI: Simone Raugei) and WSU (PI: John Peters), with key theoretical support provided by PNNL. This work will employ a comprehensive study of the redox sites of the complex before and after the electron transfer and examine the role of the global or local motions in modulating the chemical and physical properties of the enzyme. Within this proposal, we will: (1) verify the important residues for the electron transfer; (2) study the dynamical behaviors of the complex in different nucleotide-binding states and with the redox sites in different oxidation states, characterize the important motions for the electron transfer. This work is expected to yield insights on the biological nitrogen fixation to inform the design of more efficient synthetic catalysts for ammonia production.
Project Details
Start Date
2020-10-27
End Date
2021-09-30
Status
Closed
Released Data Link
Team
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