The first heme oxygenase-like dimetal oxidase/oxygenase (HDO) was functionally validated through coordinated spectroscopic and rapid kinetic studies of the fatty acid decarboxylase UndA. The enzyme superfamily has since been recognized to orchestrate a variety of substrate transformations for natural product biosynthesis. In this mini-review, we report on the structures and the catalytic mechanisms of the major HDO subtypes that catalyze carbon-carbon bond cleavage, N-oxygenation, multi-step rearrangements, and radical hole-hopping. A summary of the current status of the field and opportunities for decrypting the molecular basis for the mechanistic divergence of the family are highlighted.
Skirboll et al. (Sun,) studied this question.