Second-sphere tuning of analogues for the ferric-hydroperoxoheme form of Mycobacterium tuberculosis MhuD
Author:
Funder
National Institute of General Medical Sciences
National Institutes of Health
Publisher
Elsevier BV
Subject
Inorganic Chemistry,Biochemistry
Reference50 articles.
1. Unusual diheme conformation of the heme-degrading protein from Mycobacteriuim tuberculosis;Chim;J. Mol. Biol.,2010
2. Discovery and characterization of a unique mycobacterial heme acquisition system;Tullius;Proc. Natl. Acad. Sci.,2011
3. Insights on how the Mycobacterium tuberculosis heme uptake pathway can be used as a drug target;Owens;Future Med. Chem.,2013
4. A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO;Nambu;J. Biol. Chem.,2013
5. A single mutation in the Mycobacterium tuberculosis heme-degrading protein, MhuD, results in different products;Chao;Biochemistry,2019
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