Abstract
The inactive, nitrosyl bound form of Fe-type nitrile hydratase (NHase) contains two active site cysteine residues that are post-translationally modified to sulfenate (SO-) and sulfinate (SO2-) ligands. DFT and INDO/S calculations support the hypothesis that these unusual modifications play a key role in modulating the electronic absorption spectra and photoreactivity of the Fe(III) centre in the enzyme.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Binding Sites
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Cysteine / metabolism
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Hydro-Lyases / chemistry
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Hydro-Lyases / metabolism
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Hydro-Lyases / radiation effects*
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Light
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Models, Molecular
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Nonheme Iron Proteins / chemistry
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Nonheme Iron Proteins / metabolism
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Nonheme Iron Proteins / radiation effects
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Protein Processing, Post-Translational / physiology*
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Sulfenic Acids
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Sulfinic Acids
Substances
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Nonheme Iron Proteins
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Sulfenic Acids
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Sulfinic Acids
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Hydro-Lyases
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nitrile hydratase
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Cysteine