Nitric oxide dioxygenase mechanism of the truncated hemoglobin N from Mycobacterium tuberculosis

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This project seeks a detailed dissection of the nitric oxide dioxygenase (NOD) reaction of the truncated hemoglobin N (TrHbN) from the pathogenic bacterium Mycobacterium tuberculosis (Mtb). This enzyme has a potent ability to detoxify nitric oxide (-NO) into the innocuous nitrate and to protect aerobic respiration from the inhibition by -NO under oxygen (O2) and -NO concentrations prevailing in infected lesions (O2=1-4 µM; -NO = 0.1 -1 µM). TrHbN may represent a new potential drug target for therapy. Detailed insights of reaction mechanism may provide the molecular basis necessary to orient research in this direction. These mechanistic studies may also be of great interest to those working with other heme enzymes that catalyze redox reactions (peroxidase, catalase, prostaglandin synthase, cytochrome P450). The approach used is multidisciplinary and will contribute to formation of highly qualified personnel.