Associated Papers
Comparison of the crystal structure and function to wild-type and His25Ala mutant human heme oxygenase-1.
Zhou WP et al.
International Journal of Molecular Medicine, 2009
Crystal structures of the G139A, G139A-NO and G143H mutants of human heme oxygenase-1. A finely tuned hydrogen-bonding network controls oxygenase versus peroxidase activity.
Lad L et al.
Journal of Biological Inorganic Chemistry : Jbic : a Publication of the Society of Biological Inorganic Chemistry, 2005
A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1.
Fujii H et al.
Journal of the American Chemical Society, 2001
Replacement of the distal glycine 139 transforms human heme oxygenase-1 into a peroxidase.
Liu Y et al.
The Journal of Biological Chemistry, 2000
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