Literature summary for 1.8.5.3 extracted from

Bray, R.C.; Adams, B.; Smith, A.T.; Richards, R.L.; Lowe, D.J.; Bailey, S.
Reactions of dimethylsulfoxide reductase in the presence of dimethyl sulfide and the structure of the dimethyl sulfide-modified enzyme (2001), Biochemistry, 40, 9810-9820.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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)	Rhodobacter capsulatus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Molybdenum	formation of the intermediate formed by reaction of DMSOR with dimethylsulfide occurs at a redox potential that is 80 mV higher than that required for reduction of Mo(VI) to Mo(IV) in the free enzyme. In the back-assay the Mo(IV) state may at least in part be by-passed via two successive one electron-reactions of the intermediate with the electron-acceptor	Rhodobacter capsulatus

Organism

Organism	UniProt	Comment	Textmining
Rhodobacter capsulatus	Q52675	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	formation of the intermediate formed by reaction of DMSOR with dimethylsulfide occurs at a redox potential that is 80 mV higher than that required for reduction of Mo(VI) to Mo(IV) in the free enzyme. In the back-assay the Mo(IV) state may at least in part be by-passed via two successive one electron-reactions of the intermediate with the electron-acceptor	Rhodobacter capsulatus	?	-	?

Synonyms

Synonyms	Comment	Organism
DMSOR	-	Rhodobacter capsulatus

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Release 2023.1 (January 2023)