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Author(s): Lavinia A Carabet
Many globins convert ^(•)NO to innocuous NO(3)^(-) through their nitric oxide dioxygenase (NOD) activity. Mycobacterium tuberculosis fights the oxidative and nitrosative stress imposed by its host (the toxic effects of O(2)^(•-) and ^(•)NO species and their...
Article GUID: 28835102
Title: | Mechanism of the Nitric Oxide Dioxygenase Reaction of Mycobacterium tuberculosis Hemoglobin N |
Authors: | Lavinia A Carabet |
Link: | https://pubmed.ncbi.nlm.nih.gov/28835102/ |
DOI: | 10.1021/acs.jpcb.7b06494 |
Category: | J Phys Chem B |
PMID: | 28835102 |
Dept Affiliation: | CERMM
1 Department of Chemistry and Biochemistry and Centre for Research in Molecular Modeling (CERMM), Concordia University , Montréal, Québec, Canada H4B 1R6. |
Description: |
Many globins convert ^(•)NO to innocuous NO(3)^(-) through their nitric oxide dioxygenase (NOD) activity. Mycobacterium tuberculosis fights the oxidative and nitrosative stress imposed by its host (the toxic effects of O(2)^(•-) and ^(•)NO species and their OONO^(-) and ^(•)NO(2) derivatives) through the action of truncated hemoglobin N (trHbN), which catalyzes the NOD reaction with one of the highest rates among globins. The general NOD mechanism comprises the following steps: binding of O(2)... |