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Literature summary for 1.8.2.1 extracted from

  • Kalimuthu, P.; Kappler, U.; Bernhardt, P.V.
    Catalytic voltammetry of the molybdoenzyme sulfite dehydrogenase from Sinorhizobium meliloti (2014), J. Phys. Chem. B, 118, 7091-7099 .
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
periplasm
-
Sinorhizobium meliloti
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mo4+ molybdenum enzyme. Sulfite oxidizing enzymes (regardless of origin) share a common active site comprising a dioxido-MoVI moiety chelated by a molybdopterin dithiolene ligand in addition to a cysteinyl S-donor. The equatorial oxido ligand is the one transferred to sulfite during its 2-electron O-atom transfer reaction Sinorhizobium meliloti
additional information the enzyme bears no heme cofactor Sinorhizobium meliloti

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
78000
-
-
Sinorhizobium meliloti

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
sulfite + 2 ferricytochrome c + H2O Sinorhizobium meliloti
-
sulfate + 2 ferrocytochrome c + 2 H+
-
?

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti
-
-
-

Reaction

Reaction Comment Organism Reaction ID
sulfite + 2 ferricytochrome c + H2O = sulfate + 2 ferrocytochrome c + 2 H+ mechanism of electrochemically mediated, enzyme SorT-catalyzed sulfite oxidation Sinorhizobium meliloti

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.4
-
pH 8.0, 22°C, with horse heart cytochrome c Sinorhizobium meliloti
33.4
-
pH 8.0, 22°C, with SorU Sinorhizobium meliloti
470
-
pH 8.0, 22°C, with ferricyanide Sinorhizobium meliloti

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information favorable protein-protein interactions between SorT and c-type cytochrome SorU, i.e. Smc04048, lead to productive electron transfer and catalytic activity. No activity with ferrous horse heart cytochrome c, and no activity with O2 as an sulfite oxidase Sinorhizobium meliloti ?
-
?
sulfite + 2 ferricytochrome c + H2O
-
Sinorhizobium meliloti sulfate + 2 ferrocytochrome c + 2 H+
-
?
sulfite + 2 ferrocene methanol + H2O
-
Sinorhizobium meliloti sulfate + 2 reduced ferrocene methanol + 2 H+
-
?

Subunits

Subunits Comment Organism
homodimer
-
Sinorhizobium meliloti

Synonyms

Synonyms Comment Organism
SorT
-
Sinorhizobium meliloti

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Sinorhizobium meliloti

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
22
-
20 min, inactivation Sinorhizobium meliloti

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
the lack of a plateau prevents the determination of a genuine pH optimum, an apparently linear decrease in activity as a function of pH is not interpretable by standard models of pH-dependent enzyme activity which predict sigmoidal or bell-shaped profiles Sinorhizobium meliloti
8
-
assay at Sinorhizobium meliloti

pH Range

pH Minimum pH Maximum Comment Organism
6 11 the greatest loss in activity occurs while the enzyme is at pH 10, while in the range above pH 6 and below pH 9 there is no significant variation, inactivation at pH 11.0 Sinorhizobium meliloti

pH Stability

pH Stability pH Stability Maximum Comment Organism
11
-
irreversible time-dependent loss of catalytic activity Sinorhizobium meliloti

Cofactor

Cofactor Comment Organism Structure
cytochrome c c-type cytochrome SorU, i.e. Smc04048 Sinorhizobium meliloti
additional information ferrocene methanol (in its oxidized ferrocenium form) is utilized as an artificial electron acceptor for the catalytic SorT sulfite oxidation reaction Sinorhizobium meliloti