Fe-type nitrile hydratase

Isao Endo, Masaki Nojiri, Masanari Tsujimura, Masayoshi Nakasako, Shigehiro Nagashima, Masafumi Yohda, Masafumi Odaka

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112 Citations (Scopus)


The characteristic features of Fe-type nitrile hydratase (NHase) from Rhodococcus sp. N-771 are described. Through the biochemical analyses, we have found that nitric oxide (NO) regulates the photoreactivity of this enzyme by association with the non-heme iron center and photoinduced dissociation from it. The regulation is realized by a unique structure of the catalytic non-heme iron center composed of post-translationally modified cysteine-sulfinic (Cys-SO2H) and -sulfenic acids (Cys-SOH). To understand the biogenic mechanism and the functional role of these modifications, we constructed an over-expression system of whole NHase and individual subunits in Escherichia coli. The results of the studies on several recombinant NHases have shown that the Cys-SO2H oxidation of αC112 is indispensable for the catalytic activity of Fe-type NHase.

Original languageEnglish
Pages (from-to)247-253
Number of pages7
JournalJournal of Inorganic Biochemistry
Issue number4
Publication statusPublished - 2001 Jan 1
Externally publishedYes


  • Cysteine-sulfenic acid
  • Cysteine-sulfinic acid
  • Nitrile hydratase
  • Non-heme iron
  • Post-translational modification

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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    Endo, I., Nojiri, M., Tsujimura, M., Nakasako, M., Nagashima, S., Yohda, M., & Odaka, M. (2001). Fe-type nitrile hydratase. Journal of Inorganic Biochemistry, 83(4), 247-253. https://doi.org/10.1016/S0162-0134(00)00171-9