A widely distributed diheme enzyme from Burkholderia that displays an atypically stable bis-Fe(IV) state
Author:
Publisher
Springer Science and Business Media LLC
Subject
General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry
Link
http://www.nature.com/articles/s41467-019-09020-4.pdf
Reference59 articles.
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3. Poulos, T. L. Heme enzyme structure and function. Chem. Rev. 114, 3919–3962 (2014).
4. Shimizu, H. et al. Crystal structure of Nitrosomonas europaea cytochrome c peroxidase and the structural basis for ligand switching in bacterial di-heme peroxidases. Biochemistry 40, 13483–13490 (2001).
5. Wang, Y. et al. MauG, a novel diheme protein required for tryptophan tryptophylquinone biogenesis. Biochemistry 42, 7318–7325 (2003).
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