- 期刊
半胱胺酸雙加氧酶 (Cysteine Dioxygenase)之功能與介紹及其模型化合物的研究與發展
Introduction of Cysteine Dioxygenase: Structural Biology, Proposed Reaction Mechanisms and Biomimetic Model Complexes
摘要
在多采多姿的自然界裡，生命的存在背後隱含了一連串複雜的化學反應，生物體為維持生命機能的恆定需倚賴各種具專一性的酵素參與催化，過多或過少都會影響生理平衡。於此，我們特別針對在生物體中一種特別的酵素-半胱胺酸雙加氧酶 (Cysteine Dioxygenase, CDO) 加以介紹，CDO 是一種非血基質鐵的無機金屬酵素，在目前研究中已發現此酵素會參與人體半胱胺酸的加氧反應並與多種罕見疾病的發生有關，化學家為了更了解CDO 的神秘面紗，除了利用儀器解析此酵素的化學性質外，同時也建立了CDO 酵素的模型化合物，以研究CDO 的立體結構及解析其在催化時的反應機制。利用生物無機化學技術在瞭解生命體複雜的化學反應後，將能解決人類在醫學上碰到的難題並能提高其在科學上的相關應用性。
並列摘要
There is a variety of metalloenzymes in the biological system. The organisms use them to maintain their life. Herein, we introduce a special enzyme: Cysteine Dioxygenase (CDO); CDO is a non-heme iron enzyme, which can convert cysteine (Cys) into cysteine sulfinic acid (CSA). This conversion plays an important role in cysteine catabolism in mammalian tissue. Deficiency of CDO has been correlated with Alzheimer’s, Parkinson’s and other neurological disorders. Structural comparison from the typical non-hemeFe(II) dioxygenases to CDO, the coordination sphere of the Fe in CDO deviates fromthe fac-2-Histeines-1-carboxylate to a 3-Histeines facial triad. Themechanistic information of CDO, involves in O2 activation to generate Fe(III)-O2 − or further leading to the formation of Fe(IV) = O species, is still not clear. Biomimetic studies suggest the S-oxygenation mediatedby an Fe(II)-SR complex and O2 is expectable.
並列關鍵字
Cysteine dioxygenase ； CDO ； Cysteine sulfinic acid ； CSA ； Cysteine ； Cys ； Bioinorganic chemistry延伸閱讀
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