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McAndrew et al. (1) report the crystal structure of NOV1, a stilbene-cleaving carotenoid cleavage oxygenase (CCO), in substrate-free and substrate/product-bound forms, all of which with dioxygen (O2) bound to the nonheme iron center of the enzyme. In mononuclear nonheme iron enzymes studied to date, the Fe–O2 interaction is strongly promoted by the binding of organic substrate/cofactor at or near the iron center (2), limiting formation of potentially detrimental reactive oxygen species (3). This proposed nonsequential substrate binding in NOV1 deviates from the current paradigm of O2 activation by nonheme iron enzymes. The substrate-free NOV1 structure features O2 bound side-on to iron, modeled based on an elongated electron density peak. However, the strength of this elongated peak is nonuniform, in contrast to other side-on Fe–O2 complexes (4, 5), as reflected by the disparate B-factors for the two oxygen atoms …

Reappraisal of dioxygen binding in NOV1 crystal structures