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 | |
| Publication status | Published - 2001 |
| Externally published | Yes |
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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
Fe-type nitrile hydratase. / Endo, Isao; Nojiri, Masaki; Tsujimura, Masanari; Nakasako, Masayoshi; Nagashima, Shigehiro; Yohda, Masafumi; Odaka, Masafumi.
In: Journal of Inorganic Biochemistry, Vol. 83, No. 4, 2001, p. 247-253.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Fe-type nitrile hydratase
AU - Endo, Isao
AU - Nojiri, Masaki
AU - Tsujimura, Masanari
AU - Nakasako, Masayoshi
AU - Nagashima, Shigehiro
AU - Yohda, Masafumi
AU - Odaka, Masafumi
PY - 2001
Y1 - 2001
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
UR - http://www.scopus.com/inward/record.url?scp=0035117272&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0035117272&partnerID=8YFLogxK
U2 - 10.1016/S0162-0134(00)00171-9
DO - 10.1016/S0162-0134(00)00171-9
M3 - Article
VL - 83
SP - 247
EP - 253
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
SN - 0162-0134
IS - 4
ER -