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
N1 - Funding Information:
We gratefully acknowledge Drs. T. Noguchi, M. Hoshino, J. Honda, N. Dohmae, H. Nakayama, K. Takio, N. Kamiya, S.R. Piersma, T. Nagamune, M. Kobayashi, H. Hori, T. Nishino and many students for their energetic contribution to these studies. We thank Dr. I.-S. Lee for valuable discussion and suggestions. We also thank the Biodesign Research Program, SR Structural Biology Program, Essential Chemistry Project and Promotion of Research in RIKEN, and to Grants-in Aid for Scientific Research on Priority (11116232) from the Ministry of Education, Science, Sports and Culture of Japan for their financial support.
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
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U2 - 10.1016/S0162-0134(00)00171-9
DO - 10.1016/S0162-0134(00)00171-9
M3 - Article
C2 - 11293544
AN - SCOPUS:0035117272
VL - 83
SP - 247
EP - 253
JO - Journal of Inorganic Biochemistry
JF - Journal of Inorganic Biochemistry
SN - 0162-0134
IS - 4
ER -