Multi-scale investigation of the nitrogen fixation mechanism of Mo-dependent nitrogenase
EMSL Project ID
48288
Abstract
We propose to use EMSL NMR and supercomputing resources to gain a molecular level understanding of how substrate binding, electron, and proton delivery is controlled by the nitrogenase metalloenzyme to synthesize ammonia (NH3) from dinitrogen (N2). This research is a key component of the DOE Basic Energy Sciences Physical Biosciences proposal at PNNL, aimed at characterizing key biochemical and biophysical features of enzymatic processes and translate catalytic principles from enzymes' activity to synthetic robust catalytic platforms. We propose to use EMSL NMR and multi-scale computational studies to (1) test reaction pathways, calculate structures and energy profiles for N2 reduction intermediates, and (2) characterize large-amplitude protein fluctuations gating the electron transport steps. Characterization of structural, dynamic and thermodynamic aspects of ammonia synthesis by nitrogenase is expected to yield insights that will inform the development of functional biomimetic catalysts, which are more efficient and environmentally friendly than industrial processes currently in use.
Project Details
Project type
Large-Scale EMSL Research
Start Date
2014-10-01
End Date
2016-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members