EC Number   |
|---|
   1.8.5.3 | damaged enzyme form derived from an intermediate formed by reaction of DMSOR with dimethylsulfide and reaction with oxygen, to 2.0 A resolution. All four thiolate ligands and Ogamma of serine-147 remain coordinated to molybdenum, there are no terminal oxygen ligands and molybdenum is Mo(VI) |
| 1.8.5.3 | oxidized Mo(VI)-form, to 3.5 A resolution. Presence of a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states |
| 1.8.5.3 | protein with tungsten in place of molybdenum, to 2.0 A resolution |
| 1.8.5.3 | to 1.88 A resolution, space group P41212. Spherical protein, consists of four domains with a funnel-like cavity that leads to the freely accessible metal-ion redox center. The bis(molybdopterin guanine dinucleotide) molybdenum cofactor of the single chain protein has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center |
| 1.8.5.3 | X-ray absorption spectroscopic analysis of the molybdenum active site of Escherichia coli dimethyl sulfoxide reductase contained within its native membranes.The oxidized active site has four Mo-S ligands at 2.43 A, one Mo=O at 1.71 A, and a longer Mo-O at 1.90 A. The oxidized enzyme is a monooxomolybdenum(VI) species coordinated by two molybdopterin dithiolenes and a serine. Results suggest that the form found in vivo is the monooxobis(molybdopterin) species |
| 1.8.5.3 | x-ray absorption spectroscopy study. Dimethyl sulfoxide reductase reduced with trimethylarsine is structurally analogous to the physiologically relevant dimethyl sulfide reduced dimethyl suldfoxide reductase. These species should be regarded as formal MoIV species with a classical coordination complex of trimethylarsine oxide, with no special structural distortions. The similarity of the trimethylarsine and dimethyl sulfide complexes suggests that the dimethyl sulfide reduced enzyme possesses a classical coordination of DMSO with no special elongation of the S-O bond |
