CrII Reactivity of Taurine/α-Ketoglutarate Dioxygenase
Author:
Affiliation:
1. Departments of Microbiology & Molecular Genetics and Biochemistry & Molecular Biology, Michigan State University, East Lansing, Michigan 48824-4320
Publisher
American Chemical Society (ACS)
Subject
Inorganic Chemistry,Physical and Theoretical Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/ic700383q
Reference41 articles.
1. Characterization of α-Ketoglutarate-dependent Taurine Dioxygenase from Escherichia coli
2. Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes
3. Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins
4. The diverse and pervasive chemistries of the α-keto acid dependent enzymes
5. Non-Heme Fe(IV)–Oxo Intermediates
Cited by 3 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. Spectroscopic analyses of 2-oxoglutarate-dependent oxygenases: TauD as a case study;JBIC Journal of Biological Inorganic Chemistry;2016-11-03
2. Metal and substrate binding to an Fe(II) dioxygenase resolved by UV spectroscopy with global regression analysis;Analytical Biochemistry;2010-04
3. Chapter 3. Transient Iron Species in the Catalytic Mechanism of the Archetypal α-Ketoglutarate-Dependent Dioxygenase, TauD;Iron-Containing Enzymes
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