Fe-type nitrile hydratase

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

研究成果: Article査読

115 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)247-253
ページ数7
ジャーナルJournal of Inorganic Biochemistry
83
4
DOI
出版ステータスPublished - 2001
外部発表はい

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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