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Related Experiment Videos

Fe-type nitrile hydratase.

I Endo1, M Nojiri, M Tsujimura

  • 1Biochemical Systems Laboratory, The Institute of Physical and Chemical Research (RIKEN), Wako-shi, Saitama, Japan. endo@cel.riken.go.jp

Journal of Inorganic Biochemistry
|April 11, 2001
PubMed
Summary
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Nitric oxide (NO) uniquely regulates Fe-type nitrile hydratase (NHase) photoreactivity via its non-heme iron center. Specific cysteine modifications are essential for NHase catalytic activity.

Area of Science:

  • Biochemistry
  • Enzymology
  • Structural Biology

Background:

  • Fe-type nitrile hydratase (NHase) from Rhodococcus sp. N-771 exhibits unique catalytic features.
  • Nitric oxide (NO) is identified as a regulator of NHase photoreactivity.

Purpose of the Study:

  • To elucidate the mechanism of NO regulation on Fe-type NHase.
  • To understand the biogenic mechanism and functional role of unique post-translational modifications in the catalytic non-heme iron center.

Main Methods:

  • Biochemical analyses were performed to study enzyme regulation.
  • An over-expression system for whole NHase and individual subunits was constructed in Escherichia coli.
  • Studies were conducted on several recombinant NHases.

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Main Results:

  • Nitric oxide (NO) regulates NHase photoreactivity through binding and photoinduced dissociation from the non-heme iron center.
  • The catalytic non-heme iron center features unique cysteine-sulfinic (Cys-SO2H) and cysteine-sulfenic (Cys-SOH) acid modifications.
  • The Cys-SO2H oxidation of alphaC112 was found to be indispensable for Fe-type NHase catalytic activity.

Conclusions:

  • The study reveals a novel NO-mediated regulatory mechanism for Fe-type NHase.
  • Post-translational modifications, specifically Cys-SO2H oxidation, are critical for NHase function.
  • Understanding these mechanisms provides insights into metalloenzyme regulation and catalysis.