Carbon Monoxide Adducts of KatG and KatG(S315T) as Probes of the Heme Site and Isoniazid Binding
Author:
Affiliation:
1. Department of Chemistry, North Dakota State University, Fargo, North Dakota 58105, and Hematology Research, Department of Biochemistry and Molecular Biology, Mayo Clinic and Foundation, Rochester, Minnesota 55905
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi010369g
Reference62 articles.
Cited by 16 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. Crystal structure of the catalase–peroxidase KatG W78F mutant from Synechococcus elongatus PCC7942 in complex with the antitubercular pro‐drug isoniazid;FEBS Letters;2014-12-03
2. Heterogeneous Kinetics of the Carbon Monoxide Association and Dissociation Reaction to Nitrophorin 4 and 7 Coincide with Structural Heterogeneity of the Gate-Loop;Journal of the American Chemical Society;2012-06-06
3. Heme-Based Sensing by the Mammalian Circadian Protein CLOCK;Inorganic Chemistry;2010-07-12
4. How Active-Site Protonation State Influences the Reactivity and Ligation of the Heme in Chlorite Dismutase;Journal of the American Chemical Society;2010-03-31
5. Acyl radical addition to pyridine: multiorbital interactions;Tetrahedron;2009-09
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