Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms

Shigehiro Nagashima, Masayoshi Nakasako, Naoshi Dohmae, Masanari Tsujimura, Koji Takio, Masafumi Odaka, Masafumi Yohda, Nobuo Kamiya, Isao Endo

Research output: Contribution to journalLetter

313 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)347-351
Number of pages5
JournalNature structural biology
Volume5
Issue number5
DOIs
Publication statusPublished - 1998 May
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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    Nagashima, S., Nakasako, M., Dohmae, N., Tsujimura, M., Takio, K., Odaka, M., Yohda, M., Kamiya, N., & Endo, I. (1998). Novel non-heme iron center of nitrile hydratase with a claw setting of oxygen atoms. Nature structural biology, 5(5), 347-351. https://doi.org/10.1038/nsb0598-347