Fe-type nitrile hydratase

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

doi:10.1016/S0162-0134(00)00171-9

Fe-type nitrile hydratase

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

Department of Physics

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112 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	247-253
Number of pages	7
Journal	Journal of Inorganic Biochemistry
Volume	83
Issue number	4
DOIs	https://doi.org/10.1016/S0162-0134(00)00171-9
Publication status	Published - 2001 Jan 1

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Keywords

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

ASJC Scopus subject areas

Biochemistry
Inorganic Chemistry

Cite this

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

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abstract = "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.",

keywords = "Cysteine-sulfenic acid, Cysteine-sulfinic acid, Nitrile hydratase, Non-heme iron, Post-translational modification",

author = "Isao Endo and Masaki Nojiri and Masanari Tsujimura and Masayoshi Nakasako and Shigehiro Nagashima and Masafumi Yohda and Masafumi Odaka",

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AU - Endo, Isao

AU - Nojiri, Masaki

AU - Tsujimura, Masanari

AU - Nakasako, Masayoshi

AU - Nagashima, Shigehiro

AU - Yohda, Masafumi

AU - Odaka, Masafumi

PY - 2001/1/1

Y1 - 2001/1/1

N2 - 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.

AB - 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.

KW - Cysteine-sulfenic acid

KW - Cysteine-sulfinic acid

KW - Nitrile hydratase

KW - Non-heme iron

KW - Post-translational modification

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AN - SCOPUS:0035117272

VL - 83

SP - 247

EP - 253

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

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10.1016/S0162-0134(00)00171-9