3ELN
A Putative Fe2+-bound Persulfenate Intermediate in Cysteine Dioxygenase
Summary for 3ELN
| Entry DOI | 10.2210/pdb3eln/pdb |
| Related | 2b5h 2gh2 |
| Descriptor | Cysteine dioxygenase type 1, FE (II) ION, S-HYDROPEROXYCYSTEINE, ... (4 entities in total) |
| Functional Keywords | peroxysulfenate, non-heme dioxygenases, fe2+ metalloenzyme, cysteine, taurine, thioether, dioxygenase, iron, metal-binding, oxidoreductase, phosphoprotein, thioether bond |
| Biological source | Rattus norvegicus (brown rat,rat,rats) |
| Total number of polymer chains | 1 |
| Total formula weight | 23267.89 |
| Authors | Simmons, C.R.,Stipanuk, M.H.,Karplus, P.A. (deposition date: 2008-09-22, release date: 2008-10-21, Last modification date: 2024-02-21) |
| Primary citation | Simmons, C.R.,Krishnamoorthy, K.,Granett, S.L.,Schuller, D.J.,Dominy, J.E.,Begley, T.P.,Stipanuk, M.H.,Karplus, P.A. A putative Fe2+-bound persulfenate intermediate in cysteine dioxygenase. Biochemistry, 47:11390-11392, 2008 Cited by PubMed 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. PubMed: 18847220DOI: 10.1021/bi801546n PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.42 Å) |
Structure validation
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