The role of post-translational modification in the photoregulation of Fe-type nitrile hydratase |
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| Authors: | Greene Shannon N Chang Christopher H Richards Nigel G J |
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| Institution: | Department of Chemistry, University of Florida, Gainesville, FL 32611, USA. |
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| 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. |
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