CL : Vol. 37 (2008) , No. 7 p.672

Structural and Functional Model Systems for Analysis of the Active Center of Nitrile Hydratase

Takuma Yano¹⁾, Tomohiro Ozawa¹⁾ and Hideki Masuda¹⁾

1) Graduate School of Engineering, Nagoya Institute of Technology

(Received March 7, 2008)

The unique active site structure of nitrile hydratase (NHase) has a central metal ion (Co^III or Fe^III) 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 (Co<sup>III</sup> or Fe<sup>III</sup>) is surrounded with two amide nitrogens in peptide backbone, one cysteine sulfur and two oxidized cysteine sulfurs (Cys–SO and Cys–SO<sub>2</sub>) 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.

We focused a unique active site structure of nitrile hydratase (NHase), where the central metal ion (Co^III or Fe^III) 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.