A putative Fe2+-bound persulfenate intermediate in cysteine dioxygenase.

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

Biochemistry

journal_title

Biochemistry

authors

Simmons CR,Krishnamoorthy K,Granett SL,Schuller DJ,Dominy JE Jr,Begley TP,Stipanuk MH,Karplus PA

doi

10.1021/bi801546n

subject

Has Abstract

pub_date

2008-11-04 00:00:00

pages

11390-2

issue

44

eissn

0006-2960

issn

1520-4995

journal_volume

47

pub_type

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