<sup>19</sup>F NMR Reveals the Dynamics of Substrate Binding and Lid Closure for Iodotyrosine Deiodinase as a Complement to Steady-State Kinetics and Crystallography-Reference-Cited by-同舟云学术

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¹⁹F NMR Reveals the Dynamics of Substrate Binding and Lid Closure for Iodotyrosine Deiodinase as a Complement to Steady-State Kinetics and Crystallography

Published:2024-08-13 Issue:17 Volume:63 Page:2225-2232
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Greenberg Harrison C.¹,Majumdar Ananya²,Cheema Ekroop Kaur³,Kozyryev Anton³,Rokita Steven E.¹³^ORCID

Affiliation:

1. Chemistry–Biology Interface Graduate Training Program, Johns Hopkins University, 3400 N. Charles Street, Baltimore, Maryland 21218, United States

2. Biomolecular NMR Center, Johns Hopkins University, 3400 N. Charles Street, Baltimore, Maryland 21218, United States

3. Department of Chemistry, Johns Hopkins University, 3400 N. Charles Street, Baltimore, Maryland 21218, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.4c00243

Reference44 articles.

1. A Perspective on Enzyme Catalysis

2. Protein Motions Promote Catalysis

3. Protein Conformational Populations and Functionally Relevant Substates

4. The role of dynamic conformational ensembles in biomolecular recognition

5. A Dynamic Knockout Reveals That Conformational Fluctuations Influence the Chemical Step of Enzyme Catalysis

Cited by 1 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. Polar Interactions between Substrate and Flavin Control Iodotyrosine Deiodinase Function;Biochemistry;2024-08-30

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