Computational characterization of FeFe-Hydrogenase catalytic species
EMSL Project ID
50638
Abstract
We propose to use EMSL supercomputing resources to gain a molecular level understanding of the catalytic mechanism of the interconversion of H2 into electrons and protons and vice versa at the active site of Clostridium pasteurianum [FeFe]-hydrogenase (CpI-H2ase). The projects 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 characterization of the catalytic intermediates in different oxidation states and the role of the enzyme scaffold in modulating the chemical and physical features of the process. Within this proposal we will: (1) study the dynamical behavior of the enzyme in different oxidation states of the active site and the associated FeS clusters involved in the electron transport, focusing on identifying significant conformational changes near the active site and long range couplings (allosteric interactions) triggered by changes at the catalytic center; (2) calculate the structures and energetics of the individual steps of the catalytic cycle; (3) characterize and verify the spectroscopic signatures of the newly experimentally proposed intermediates in an effort to elucidate their role in the catalysis.
Project Details
Start Date
2018-11-19
End Date
2019-09-30
Status
Closed
Released Data Link
Team
Principal Investigator
Team Members