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A new approach to possible substrate binding mechanisms for nitrile hydratase

A Ozlem Taştan Bishop1, Trevor Sewell

  • 1Department of Biotechnology, University of the Western Cape, Bellville 7535, South Africa. ozlem@tuks.co.za

Biochemical and Biophysical Research Communications
|March 17, 2006
PubMed
Summary

Normal mode analysis combined with cavity calculations reveals dynamic mechanisms in nitrile hydratase (NHase) enzyme structures. This study proposes "breathing" and "flip-flop" motions crucial for substrate binding in NHase.

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