Outer-Sphere Tyrosine 159 within the 3-Mercaptopropionic Acid Dioxygenase S-H-Y Motif Gates Substrate-Coordination Denticity at the Non-Heme Iron Active Site

Author:

Sardar Sinjinee1,Weitz Andrew2,Hendrich Michael P.2ORCID,Pierce Brad S.3ORCID

Affiliation:

1. Department of Chemistry and Biochemistry, The University of Texas at Arlington, 700 Planetarium Place, Arlington, Texas 76019, United States

2. Department of Chemistry, Carnegie Mellon University, 4400 Fifth Avenue, Pittsburgh, Pennsylvania 15213, United States

3. Department of Chemistry and Biochemistry, University of Alabama, 250 Hackberry Lane, Tuscaloosa, Alabama 35487, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Cited by 12 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. Thiol dioxygenases: from structures to functions;Trends in Biochemical Sciences;2024-06

2. Improved resolution of 3-mercaptopropionate dioxygenase active site provided by ENDOR spectroscopy offers insight into catalytic mechanism;Journal of Biological Chemistry;2024-04

3. Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine;Angewandte Chemie International Edition;2024-01-11

4. Enzyme‐Catalyzed Oxidative Degradation of Ergothioneine;Angewandte Chemie;2024-01-11

5. 3‐Mercaptopropionate Dioxygenase (MDO);Encyclopedia of Inorganic and Bioinorganic Chemistry;2023-04-28

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