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Electron Transfer of Nitrogenase Complex


EMSL Project ID
51177

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 proposal at PNNL and the BETCy EFRC led by WSU, with key theoretical support provided by PNNL. This work will employ a comprehensive study of the redox sites of the complex in different oxidation states 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) identify the electron transfer pathways, calculate the energy profiles 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; (3) verify and propose the important residues 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
2019-10-08
End Date
2020-09-30
Status
Closed

Team

Principal Investigator

Simone Raugei
Institution
Pacific Northwest National Laboratory

Team Members

Conrad Johnston
Institution
Pacific Northwest National Laboratory

Qi Huang
Institution
Pacific Northwest National Laboratory

Bojana Ginovska
Institution
Pacific Northwest National Laboratory