Abstract
The iron-containing nitrile hydratase (NHase) is a photoreactive enzyme that is inactivated in the dark because of persistent association with NO and activated by photo-dissociation of NO. The crystal structure at 1.7 Å resolution and mass spectrometry revealed the structure of the non-heme iron catalytic center in the nitrosylated state. Two Cys residues coordinated to the iron were post-translationally modified to Cys-sulfenic and -sulfinic acids. Together with another oxygen atom of the Ser ligand, these modifications induced a claw setting of oxygen atoms capturing an NO molecule. This unprecedented structure is likely to enable the photo-regulation of NHase and will provide an excellent model for designing photo-controllable chelate complexes and, ultimately, proteins.
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Nagashima, S., Nakasako, M., Dohmae, N. et al. Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms. Nat Struct Mol Biol 5, 347–351 (1998). https://doi.org/10.1038/nsb0598-347
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DOI: https://doi.org/10.1038/nsb0598-347
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