A Structural Model for the Iron–Nitrosyl Adduct of Gentisate Dioxygenase
Author:
Affiliation:
1. Department of Chemistry Oakland University 48309‐4477 Rochester MI USA
2. Department of Chemistry The University of Michigan 48109‐1055 Ann Arbor MI USA
3. Department of Chemistry University of Rochester 14627‐0216 Rochester NY USA
Funder
National Institute of General Medical Sciences
Directorate for Mathematical and Physical Sciences
Publisher
Wiley
Subject
Inorganic Chemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/ejic.201800992
Reference47 articles.
1. Structural and biochemical characterization of gentisate 1,2-dioxygenase from Escherichia coli O157:H7
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3. Gentisate 1,2-dioxygenase from Pseudomonas. Substrate coordination to active site Fe2+ and mechanism of turnover.
4. Spontaneous release of fluoride during the dioxygenolytic cleavage of 5-fluorosalicylate by the salicylate 1,2-dioxygenase fromPseudaminobacter salicylatoxidansBN12
5. Expansion of the substrate range of the gentisate 1,2-dioxygenase from Corynebacterium glutamicum for the conversion of monohydroxylated benzoates
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