Localization of a Substrate Binding Site on the FeMo-Cofactor in Nitrogenase: Trapping Propargyl Alcohol with an α-70-Substituted MoFe Protein
Author:
Affiliation:
1. Department of Chemistry and Biochemistry, Utah State University, Logan, Utah 84322, Department of Chemistry, Northwestern University, Evanston, Illinois 60208, and Department of Biochemistry, Virginia Tech, Blacksburg, Virginia 24061
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi034595x
Reference61 articles.
Cited by 95 articles. 订阅此论文施引文献 订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献
1. Analysis of early intermediate states of the nitrogenase reaction by regularization of EPR spectra;Nature Communications;2024-05-13
2. The activating capture of N2 at the active site of Mo–nitrogenase;Dalton Transactions;2024
3. Analysis of early intermediate states of the nitrogenase reaction by Se incorporation and regularization of EPR spectra;2023-07-19
4. How thermal fluctuations influence the function of the FeMo cofactor in nitrogenase enzymes;Chem Catalysis;2023-07
5. 13C ENDOR Characterization of the Central Carbon within the Nitrogenase Catalytic Cofactor Indicates That the CFe6 Core Is a Stabilizing “Heart of Steel”;Journal of the American Chemical Society;2022-09-27
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