The influences of carbon donor ligands on biomimetic multi-iron complexes for N2 reduction
Author:
Affiliation:
1. Department of Chemistry
2. Yale University
3. New Haven
4. USA
5. Department of Chemistry and Chemical Biology
6. Baker Laboratory
7. Cornell University
8. Ithaca
Abstract
High-spin diiron alkylidenes give insight into the electronic structure and functional relevance of carbon in the FeMoco active site of nitrogenase.
Funder
National Institute of General Medical Sciences
U.S. Department of Energy
Publisher
Royal Society of Chemistry (RSC)
Subject
General Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2020/SC/D0SC03447A
Reference86 articles.
1. Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage
2. Substrate Interactions with the Nitrogenase Active Site
3. EXAFS and NRVS Reveal a Conformational Distortion of the FeMo-cofactor in the MoFe Nitrogenase Propargyl Alcohol Complex
4. Localization of a Substrate Binding Site on the FeMo-Cofactor in Nitrogenase: Trapping Propargyl Alcohol with an α-70-Substituted MoFe Protein
5. An Organometallic Intermediate during Alkyne Reduction by Nitrogenase
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