Chemistry Letters
Online ISSN : 1348-0715
Print ISSN : 0366-7022
ISSN-L : 0366-7022
Volume 37 , Issue 7
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  • Takuma Yano, Tomohiro Ozawa, Hideki Masuda
    2008 Volume 37 Issue 7 Pages 672-677
    Published: July 05, 2008
    Released: May 31, 2008
    JOURNALS RESTRICTED ACCESS
    The unique active site structure of nitrile hydratase (NHase) has a central metal ion (CoIII or FeIII) coordinated by two amide nitrogens from the peptide backbone, one cysteine sulfur and two oxidized cysteine sulfurs (Cys–SO and Cys–SO2). In this review, the biological implications of the nitrile hydration mechanism are discussed in context of model complexes prepared with the aim of understanding the unique structure of nitrile hydratase.
    We focused a unique active site structure of nitrile hydratase (NHase), where the central metal ion (CoIII or FeIII) is surrounded with two amide nitrogens in peptide backbone, one cysteine sulfur and two oxidized cysteine sulfurs (Cys–SO and Cys–SO2) as the donor set. In this review, the biological implication of the unique structure has been discussed in the relation with the nitrile hydration mechanism by using model complexes. Fullsize Image
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