View : 140 Download: 0
A chromium(III)-superoxo complex in oxygen atom transfer reactions as a chemical model of cysteine dioxygenase
- A chromium(III)-superoxo complex in oxygen atom transfer reactions as a chemical model of cysteine dioxygenase
- Cho J.; Woo J.; Nam W.
- Ewha Authors
- 남원우; 조재흥
- SCOPUS Author ID
- Issue Date
- Journal Title
- Journal of the American Chemical Society
- Journal of the American Chemical Society vol. 134, no. 27, pp. 11112 - 11115
- SCIE; SCOPUS
- Document Type
- Metal-superoxo species are believed to play key roles in oxygenation reactions by metalloenzymes. One example is cysteine dioxygenase (CDO) that catalyzes the oxidation of cysteine with O 2, and an iron(III)-superoxo species is proposed as an intermediate that effects the sulfoxidation reaction. We now report the first biomimetic example showing that a chromium(III)-superoxo complex bearing a macrocyclic TMC ligand, [Cr III(O 2)(TMC)(Cl)] +, is an active oxidant in oxygen atom transfer (OAT) reactions, such as the oxidation of phosphine and sulfides. The electrophilic character of the Cr(III)-superoxo complex is demonstrated unambiguously in the sulfoxidation of para-substituted thioanisoles. A Cr(IV)-oxo complex, [Cr IV(O)(TMC)(Cl)] +, formed in the OAT reactions by the chromium(III)-superoxo complex, is characterized by X-ray crystallography and various spectroscopic methods. The present results support the proposed oxidant and mechanism in CDO, such as an iron(III)-superoxo species is an active oxidant that attacks the sulfur atom of the cysteine ligand by the terminal oxygen atom of the superoxo group, followed by the formation of a sulfoxide and an iron(IV)-oxo species via an O-O bond cleavage. © 2012 American Chemical Society.
- Appears in Collections:
- 자연과학대학 > 화학·나노과학전공 > Journal papers
- Files in This Item:
There are no files associated with this item.
- RIS (EndNote)
- XLS (Excel)
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.