Binding of 15N-Labeled Isoniazid to KatG and KatG(S315T): Use of Two-Spin [zz]-Order Relaxation Rate for 15N−Fe Distance Determination
Author:
Affiliation:
1. Contribution from the Department of Biochemistry and Molecular Biology, Section of Hematology Research, Mayo Clinic and Foundation, Rochester, Minnesota 55905, and Faculty of Physical Chemistry, University of Belgrade, Belgrade, Yugoslavia
Publisher
American Chemical Society (ACS)
Subject
Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis
Link
https://pubs.acs.org/doi/pdf/10.1021/ja9918674
Reference38 articles.
1. Overexpression, Purification, and Characterization of the Catalase-peroxidase KatG from Mycobacterium tuberculosis
2. Evidence for Differential Binding of Isoniazid by Mycobacterium tuberculosis KatG and the Isoniazid-Resistant Mutant KatG(S315T)
3. The Requirement for Manganese and Oxygen in the Isoniazid-Dependent Inactivation of Mycobacterium tuberculosis Enoyl Reductase
4. The Role of Mn(II)-Peroxidase Activity of Mycobacterial Catalase-Peroxidase in Activation of the Antibiotic Isoniazid
5. Evidence for Isoniazid Oxidation by Oxyferrous Mycobacterial Catalase−Peroxidase
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