A putative Fe2+-bound persulfenate intermediate in cysteine dioxygenase.
Biochemistry
; 47(44): 11390-2, 2008 Nov 04.
Article
in En
| MEDLINE
| ID: mdl-18847220
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Cysteine Dioxygenase
Limits:
Animals
Language:
En
Journal:
Biochemistry
Year:
2008
Type:
Article
Affiliation country:
United States