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Literature summary for 1.8.5.3 extracted from

  • George, G.; Nelson, K.; Harris, H.; Doonan, C.; Rajagopalan, K.
    Interaction of product analogues with the active site of Rhodobacter sphaeroides dimethyl sulfoxide reductase (2007), Inorg. Chem., 46, 3097-3104.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
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Cereibacter sphaeroides

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Cereibacter sphaeroides

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides
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