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EC 1.8.5.6 Details

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EC number

1.8.5.6

Accepted name

sulfite dehydrogenase (quinone)

Reaction

sulfite + a quinone + H₂O = sulfate + a quinol

Other name(s)

soeABC (gene name)

Systematic name

sulfite:quinone oxidoreductase

Comment

This membrane-bound bacterial enzyme catalyses the direct oxidation of sulfite to sulfate in the cytoplasm. The enzyme, characterized from the bacteria Ruegeria pomeroyi and Allochromatium vinosum, is a complex that consists of a membrane anchor (SoeC) and two cytoplasmic subunits: an iron-sulfur protein (SoeB) and a molybdoprotein that contains a [4Fe-4S] iron-sulfur cluster (SoeA). cf. EC 1.8.2.1, sulfite dehydrogenase (cytochrome).

History

created 2016

EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.1 With NAD⁺ or NADP⁺ as acceptor

1.1.2 With a cytochrome as acceptor

1.1.3 With oxygen as acceptor

1.1.4 With a disulfide as acceptor

1.1.5 With a quinone or similar compound as acceptor

1.1.7 With an iron-sulfur protein as acceptor

1.1.9 With a copper protein as acceptor

1.1.98 With other, known, physiological acceptors

1.1.99 With unknown physiological acceptors

1.2 Acting on the aldehyde or oxo group of donors

1.3 Acting on the CH-CH group of donors

1.4 Acting on the CH-NH₂ group of donors

1.5 Acting on the CH-NH group of donors

1.6 Acting on NADH or NADPH

1.7 Acting on other nitrogenous compounds as donors

1.7.1 With NAD⁺ or NADP⁺ as acceptor

1.7.2 With a cytochrome as acceptor

1.7.3 With oxygen as acceptor

1.7.5 With a quinone or similar compound as acceptor

1.7.6 With a nitrogenous group as acceptor

1.7.7 With an iron-sulfur protein as acceptor

1.7.9 With a copper protein as acceptor

1.7.99 With unknown physiological acceptors

1.7.99.1 hydroxylamine reductase

1.7.99.2 created 1961, modified 1976, deleted 1992

1.7.99.3 created 1961 as EC 1.6.6.5, transferred 1964 to EC 1.7.99.3, modified 1976, deleted 2002

1.7.99.4 nitrate reductase

1.7.99.5 created 1965 as EC 1.1.1.68, transferred 1978 to EC 1.1.99.15, transferred 1980 to EC 1.7.99.5, deleted 2005

1.7.99.6 nitrous-oxide reductase

1.7.99.7 nitric-oxide reductase

1.7.99.8 hydrazine oxidoreductase

1.8 Acting on a sulfur group of donors

1.8.1 With NAD⁺ or NADP⁺ as acceptor

1.8.2 With a cytochrome as acceptor

1.8.3 With oxygen as acceptor

1.8.4 With a disulfide as acceptor

1.8.5 With a quinone or similar compound as acceptor

1.8.5.1 glutathione dehydrogenase (ascorbate)

1.8.5.2 thiosulfate dehydrogenase (quinone)

1.8.5.3 respiratory dimethylsulfoxide reductase

1.8.5.4 bacterial sulfide:quinone reductase

1.8.5.5 thiosulfate reductase (quinone)

1.8.5.6 sulfite dehydrogenase (quinone)

1.8.5.7 glutathionyl-hydroquinone reductase

1.8.5.8 eukaryotic sulfide quinone oxidoreductase

1.8.5.9 protein dithiol:quinone oxidoreductase DsbB

1.8.6 With a nitrogenous group as acceptor (deleted sub-subclass)

1.8.7 With an iron-sulfur protein as acceptor

1.8.98 With other, known, physiological acceptors

1.8.99 With unknown physiological acceptors

1.9 Acting on a heme group of donors

1.10 Acting on diphenols and related substances as donors

1.11 Acting on a peroxide as acceptor

1.12 Acting on hydrogen as donor

1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)

1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

1.15 Acting on superoxide as acceptor

1.16 Oxidizing metal ions

1.17 Acting on CH or CH₂ groups

1.18 Acting on iron-sulfur proteins as donors

1.19 Acting on reduced flavodoxin as donor

1.20 Acting on phosphorus or arsenic in donors

1.21 Catalysing the reaction X-H + Y-H = X-Y

1.21.1 With NAD⁺ or NADP⁺ as acceptor

1.21.3 With oxygen as acceptor

1.21.4 With a disulfide as acceptor

1.21.98 With other, known, physiological acceptors

1.21.99 With unknown physiological acceptors

1.22 Acting on halogen in donors

1.23 Reducing C-O-C group as acceptor

1.97 Other oxidoreductases

1.98 Enzymes using H₂ as reductant (deleted subclass)

1.99 Other enzymes using O₂ as oxidant (deleted subclass)

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Release 2023.1 (January 2023)