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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.

SUBMITTER: Simmons CR

PROVIDER: S-EPMC2684787 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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

Simmons Chad R CR Krishnamoorthy Kalyanaraman K Granett Spencer L SL Schuller David J DJ Dominy John E JE Begley Tadhg P TP Stipanuk Martha H MH Karplus P Andrew PA

Biochemistry 20081011 44

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 involv ...[more]

PMID: 18847220

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