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Literature summary for 1.8.5.3 extracted from

  • Kirk, M.L.; Kc, K.
    Molybdenum and tungsten cofactors and the reactions they catalyze (2020), Met. Ions Life Sci., 20, 313-342 .
    View publication on PubMed
Search for more literature for 1.8.5.3

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum required Rhodobacter capsulatus
Molybdenum required Cereibacter sphaeroides

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
dimethylsulfoxide + menaquinol Rhodobacter capsulatus
-
 dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol Cereibacter sphaeroides
-
 dimethylsulfide + menaquinone + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Cereibacter sphaeroides Q57366 Rhodobacter sphaeroides
-
Rhodobacter capsulatus Q52675
-
-

Reaction

Reaction Comment Organism Reaction ID
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol reaction mechanism, overview. Reactions of reduced enzyme with DMSO are biphasic in the pH 6-10 range, and reveal a fast initial substrate binding phase followed by a catalytic phase that is independent of the substrate concentration. Spectral deconvolution of the absorption spectrum over the time course of the reaction reveals contributions from four distinct species that are catalytically relevant. These include an oxidized Mo(VI) state, a one-electron reduced Mo(V) high-g split intermediate, fully reduced enzyme in the Mo(IV) state, and a reduced enzyme form with DMSO bound to the Mo site. The distorted trigonal prismatic active site structure in DMSO reductase imparts significant electronic structure contributions to enzymatic catalysis Cereibacter sphaeroides
a
dimethylsulfide + menaquinone + H2O = dimethylsulfoxide + menaquinol reaction mechanism, overview. The distorted trigonal prismatic active site structure in DMSO reductase imparts significant electronic structure contributions to enzymatic catalysis Rhodobacter capsulatus
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dimethylsulfoxide + menaquinol
-
 Rhodobacter capsulatus dimethylsulfide + menaquinone + H2O
-
 ?
dimethylsulfoxide + menaquinol
-
 Cereibacter sphaeroides dimethylsulfide + menaquinone + H2O
-
 ?

Synonyms

Synonyms Comment Organism
dimethyl sulfoxide reductase
-
 Rhodobacter capsulatus
dimethyl sulfoxide reductase
-
 Cereibacter sphaeroides
DmsA
-
 Cereibacter sphaeroides
DMSO reductase
-
 Rhodobacter capsulatus
DMSO reductase
-
 Cereibacter sphaeroides
DMSOR
-
 Rhodobacter capsulatus
DMSOR
-
 Cereibacter sphaeroides
dorA
-
 Rhodobacter capsulatus

Cofactor

Cofactor Comment Organism Structure
molybdenum cofactor pterin-based cofactor MoCo, the unique cofactor contains the ligand pyranopterin ene-1,2-dithiolate. Mechanism for mature Moco formation, overview. Bacterial DMSO reductase family enzymes possess a bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor that is obtained by adding GMP to the MPT terminal phosphates. Enzymes that belong to the DMSO reductase enzyme family possess two coordinated MPTs, with one of the MPTs adopting an SO family configuration and the other a more distorted XO enzyme family structure, role of MPT in catalysis Rhodobacter capsulatus
molybdenum cofactor pterin-based cofactor MoCo, the unique cofactor contains the ligand pyranopterin ene-1,2-dithiolate. Mechanism for mature Moco formation, overview. Bacterial DMSO reductase family enzymes possess a bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor that is obtained by adding GMP to the MPT terminal phosphates. Enzymes that belong to the DMSO reductase enzyme family possess two coordinated MPTs, with one of the MPTs adopting an SO family configuration and the other a more distorted XO enzyme family structure, role of MPT in catalysis Cereibacter sphaeroides

General Information

General Information Comment Organism
evolution the enzyme belongs to the dimethyl sulfoxide (DMSO) reductase family. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The DMSO reductase family enzymes are divided into three classes (Types I, II, and III) that are distinguished from each other by their active site structure and the nature of the donor ligand that is provided by the polypeptide. DMSO reductase family enzymes are quite diverse and not all of the enzymes in this family adhere to this general classification scheme. DMSO reductases are type III enzymes and a combination of EXAFS and high resolution X-ray crystallography shows that the oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry Rhodobacter capsulatus
evolution the enzyme belongs to the dimethyl sulfoxide (DMSO) reductase family. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The DMSO reductase family enzymes are divided into three classes (Types I, II, and III) that are distinguished from each other by their active site structure and the nature of the donor ligand that is provided by the polypeptide. DMSO reductase family enzymes are quite diverse and not all of the enzymes in this family adhere to this general classification scheme. DMSO reductases are type III enzymes and a combination of EXAFS and high resolution X-ray crystallography shows that the oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry Cereibacter sphaeroides
additional information structure-function analysis of DMSO reductases, overview. Comparison of oxygen atom transfer (OAT) reactivity in different families of canonical pyranopterin Mo enzymes , including the DMSO reductase family, the sulfite oxidase (SO) family, the xanthine oxidase (XO) family enzymes, and the formate dehydrogenases. The active site structures and the nature of the ligands bound to the metal center appear to be fine-tuned so that the reactions catalyzed by pyranopterin Mo enzymes are close to thermoneutral. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry Rhodobacter capsulatus
additional information structure-function analysis of DMSO reductases, overview. Comparison of oxygen atom transfer (OAT) reactivity in different families of canonical pyranopterin Mo enzymes, including the DMSO reductase family, the sulfite oxidase (SO) family, the xanthine oxidase (XO) family enzymes, and the formate dehydrogenases. The active site structures and the nature of the ligands bound to the metal center appear to be fine-tuned so that the reactions catalyzed by pyranopterin Mo enzymes are close to thermoneutral. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry Cereibacter sphaeroides
physiological function bacterial DMSO reductase and trimethylamine-N-oxide reductase (TMAO reductase) are of increasing environmental importance since they catalyze the oxidation of marine osmolytes and facilitate cloud formation and albedo Rhodobacter capsulatus
physiological function bacterial DMSO reductase and trimethylamine-N-oxide reductase (TMAO reductase) are of increasing environmental importance since they catalyze the oxidation of marine osmolytes and facilitate cloud formation and albedo Cereibacter sphaeroides