Abstract:
: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.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Simmons CR,Krishnamoorthy K,Granett SL,Schuller DJ,Dominy JE Jr,Begley TP,Stipanuk MH,Karplus PAdoi
10.1021/bi801546nsubject
Has Abstractpub_date
2008-11-04 00:00:00pages
11390-2issue
44eissn
0006-2960issn
1520-4995journal_volume
47pub_type
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