Key result
Review explores nitrile hydration mechanisms in model complexes to clarify unique nitrile hydratase structures.
Why the study?
The unique active site structure and nitrile hydration mechanism of nitrile hydratase require elucidation through model complexes to understand its biological implications.
Provides a review of structural and functional model systems for understanding the active center of nitrile hydratase.
Model complexes refine nitrile hydratase understanding; leaves open any clinical or biocatalytic translation.
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.
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Yano et al. (2008) conducted a review in Nitrile hydratase active site structure. Model complexes of nitrile hydratase was evaluated. This review discusses the biological implications of the nitrile hydration mechanism in the context of model complexes to understand the unique structure of nitrile hydratase.
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