Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
The common reactions of dioxygen, superoxide, and hydroperoxides with thiolates are thought to proceed via persulfenate intermediates, yet these have never been visualized. Here we report a 1.4 A resolution crystal structure of the Fe(2+)-dependent enzyme cysteine dioxygenase (CDO) containing this putative intermediate trapped in its active site pocket. The complex raises the possibility that, distinct from known dioxygenases and proposed CDO mechanisms, the Fe-proximal oxygen atom may be involved in the primary oxidation event yielding a unique three-membered Fe-S-O cyclic intermediate. A nonpolar environment of the distal oxygen would facilitate isomerization of the persulfenate to the sulfinate product.
A putative Fe2+-bound persulfenate intermediate in cysteine dioxygenase.,Simmons CR, Krishnamoorthy K, Granett SL, Schuller DJ, Dominy JE Jr, Begley TP, Stipanuk MH, Karplus PA Biochemistry. 2008 Nov 4;47(44):11390-2. Epub 2008 Oct 11. PMID:18847220[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Simmons CR, Krishnamoorthy K, Granett SL, Schuller DJ, Dominy JE Jr, Begley TP, Stipanuk MH, Karplus PA. A putative Fe2+-bound persulfenate intermediate in cysteine dioxygenase. Biochemistry. 2008 Nov 4;47(44):11390-2. Epub 2008 Oct 11. PMID:18847220 doi:10.1021/bi801546n
