Fe-type nitrile hydratase |
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Authors: | Endo I Nojiri M Tsujimura M Nakasako M Nagashima S Yohda M Odaka M |
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Affiliation: | Biochemical Systems Laboratory, The Institute of Physical and Chemical Research (RIKEN), Wako-shi, Saitama, Japan. endo@cel.riken.go.jp |
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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 alphaC112 is indispensable for the catalytic activity of Fe-type NHase. |
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