Article
Ligand binding to truncated hemoglobin N from Mycobacterium tuberculosis is strongly modulated by the interplay between the distal heme pocket residues and internal water.
The Journal of biological chemistry - 3 Oct 2008
Ouellet Yannick H, Daigle Richard, Lagüe Patrick, Dantsker David, Milani Mario, Bolognesi Martino, Friedman Joel M, Guertin Michel
Abstract excerpt
The survival of Mycobacterium tuberculosis requires detoxification of host *NO. Oxygenated Mycobacterium tuberculosis truncated hemoglobin N catalyzes the rapid oxidation of nitric oxide to innocuous nitrate with a second-order rate constant (k'(NOD) approximately 745 x 10(6) m(-1) x s(-1)), which is approximately 15-fold faster than the reaction of horse heart myoglobin. We ask what aspects of structure and/or...
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