Carbon Monoxide Binding to the Iron–Molybdenum Cofactor of Nitrogenase: a Detailed Quantum Mechanics/Molecular Mechanics Investigation
Author:
Affiliation:
1. Max-Planck-Institut für Kohlenforschung, Kaiser-Wilhelm-Platz 1, 45470 Mülheim an der Ruhr, Germany
2. Max Planck Institute for Chemical Energy Conversion, Stiftstr 34-36, 45470 Mülheim an der Ruhr, Germany
Funder
Icelandic Centre for Research
Deutsche Forschungsgemeinschaft
Max Planck society
International Max Planck Research School on Reactive Structure Analysis for Chemical Reactions (IMPRS-RECHARGE)
Publisher
American Chemical Society (ACS)
Subject
Inorganic Chemistry,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acs.inorgchem.1c02649
Reference111 articles.
1. Mechanism of Molybdenum Nitrogenase
2. X-ray Emission Spectroscopy Evidences a Central Carbon in the Nitrogenase Iron-Molybdenum Cofactor
3. Evidence for Interstitial Carbon in Nitrogenase FeMo Cofactor
4. The mechanism of Klebsiella pneumoniae nitrogenase action. Pre-steady-state kinetics of an enzyme-bound intermediate in N2 reduction and of NH3 formation
5. Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage
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