The role of post-translational modification in the photoregulation of Fe-type nitrile hydratase.
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.
Greene
Shannon N
SN
Department of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Chang
Christopher H
CH
Richards
Nigel G J
NG
D001665:Binding Sites; D003545:Cysteine / Q000378:metabolism; D006836:Hydro-Lyases / Q000737:chemistry / Q000378:metabolism / Q000528:radiation effects*; D008027:Light; D008958:Models, Molecular; D019159:Nonheme Iron Proteins / Q000737:chemistry / Q000378:metabolism / Q000528:radiation effects; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D013434:Sulfenic Acids; D013441:Sulfinic Acids
D019159:Nonheme Iron Proteins; D013434:Sulfenic Acids; D013441:Sulfinic Acids; D006836:Hydro-Lyases; C048831:nitrile hydratase; D003545:Cysteine