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Significance Oxygenases are classified into two groups, mono- and dioxygenases, which, respectively, catalyze insertion of one and two oxygen atoms of O2 into substrates. These two modes of oxygenation proceed through distinct reaction mechanisms and require totally different active site structures. For more than 60 years, oxygenase enzymes thus far have been found to catalyze either a mono- or dioxygenation reaction. This study has broken this paradigm as it clearly demonstrates that the heme-degrading enzyme fromMycobacterium tuberculosis , MhuD, catalyzes successive mono- and dioxygenation reactions within its single active site. This unprecedented bifunctionality of the single active center rationally explains the unique heme catabolites of MhuD, which have been proposed to meet the physiological demands of the pathogenic bacterium.

Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation