The role of post-translational modification in the photoregulation of Fe-type nitrile hydratase

Shannon N. Greene; Christopher H. Chang; Nigel G. J. Richards

doi:10.1039/B207027H

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The role of post-translational modification in the photoregulation of Fe-type nitrile hydratase†

Shannon N. Greene,^a Christopher H. Chang ‡^a and Nigel G. J. Richards*^a

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* Corresponding authors

^a Department of Chemistry, University of Florida, Gainesville, FL, USA
E-mail: richards@qtp.ufl.edu

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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Supplementary files

Selected structural parameters of the experimentally observed NHase active site and DFT-optimised models 1 and 2, and graphical MO representations of the calculated INDO/S spectroscopic transitions for the models discussed DOC (252K)

Article information

DOI: https://doi.org/10.1039/B207027H
Article type: Communication
Submitted: 18 Jul 2002
Accepted: 28 Aug 2002
First published: 19 Sep 2002

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Chem. Commun., 2002, 2386-2387

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The role of post-translational modification in the photoregulation of Fe-type nitrile hydratase

S. N. Greene, C. H. Chang and N. G. J. Richards, Chem. Commun., 2002, 2386 DOI: 10.1039/B207027H

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Chemical Communications

The role of post-translational modification in the photoregulation of Fe-type nitrile hydratase†

Abstract

Supplementary files

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The role of post-translational modification in the photoregulation of Fe-type nitrile hydratase

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