Characterization and Crystal Structure of a Nonheme Diiron Monooxygenase Involved in Platensimycin and Platencin Biosynthesis
Author:
Affiliation:
1. Midwest Center for Structural Genomics and Structural Biology Center, Biosciences Division, Argonne National Laboratory, Argonne, Illinois 60439, United States
2. Department of Biosciences, Rice University, Houston, Texas 77030, United States
Funder
National Institute of General Medical Sciences
Guangdong Academy of Science, Guangzhou, P. R. China
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/jacs.9b06183
Reference30 articles.
1. Soluble Methane Monooxygenase
2. Dioxygen Activation by Nonheme Diiron Enzymes: Diverse Dioxygen Adducts, High-Valent Intermediates, and Related Model Complexes
3. Diiron monooxygenases in natural product biosynthesis
4. A family of diiron monooxygenases catalyzing amino acid beta-hydroxylation in antibiotic biosynthesis
5. CmlI is an N-oxygenase in the biosynthesis of chloramphenicol
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