Greene Shannon N, Chang Christopher H, Richards Nigel G J
Department of Chemistry, University of Florida, Gainesville, FL 32611, USA.
Chem Commun (Camb). 2002 Oct 21(20):2386-7. doi: 10.1039/b207027h.
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.
铁型腈水合酶(NHase)的无活性亚硝酰结合形式含有两个活性位点半胱氨酸残基,这些残基在翻译后被修饰为亚磺酸盐(SO-)和亚磺酸盐(SO2-)配体。密度泛函理论(DFT)和间略微分重叠/全略微分重叠(INDO/S)计算支持这样的假设,即这些不寻常的修饰在调节酶中Fe(III)中心的电子吸收光谱和光反应性方面起关键作用。