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Letter
Nature structural biology  5, 347 - 351 (1998)
doi:10.1038/nsb0598-347

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

Shigehiro Nagashima1, 2, Masayoshi Nakasako3, Naoshi Dohmae1, Masanari Tsujimura1, 4, Koji Takio1, Masafumi Odaka1, Masafumi Yohda1, Nobuo Kamiya1, 5 & Isao Endo1, 6

  1The Institute of Physical and Chemical Research (RIKEN), Hirosawa 2-1, Wako, Saitama 351-0198, Japan.

  2Present address: Namba Protonic Nanomachine Project, ERATO, JST, Hikaridai 3-4, Seika-cho, Soraku-gun, Kyoto 619-0237, Japan.

  3PRESTO, JST and Institute for Molecular and Cellular Biosciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan.

  4Graduate School of Science and Engineering, Saitama University, Shimo-Okubo 251, Urawa, Saitama 338-0825, Japan.

  5TARA Sakabe Project, University of Tsukuba, Tennodai 1-1-1, Tsukuba-city, Ibaraki 305-0006, Japan.

  6email: endo@cel.riken.go.jp

 All of the authors contributed equally to this work.

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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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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