Sulfite oxidase

SUOX
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1MJ4
Identifiers
Aliases	SUOX, entrez:6821, sulfite oxidase
External IDs	OMIM: 606887; MGI: 2446117; HomoloGene: 394; GeneCards: SUOX; OMA:SUOX - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	56,006,641 bp
Gene location (Mouse)
Chr.	Chromosome 10 (mouse)
End	128,509,942 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; right adrenal gland; ; right adrenal cortex; ; human kidney; ; left adrenal gland; ; left adrenal cortex; ; mucosa of transverse colon; ; muscle of thigh; ; apex of heart; ; renal medulla;
	Top expressed in
	seminal vesicula; ; gastrula; ; pyloric antrum; ; mucous cell of stomach; ; left lobe of liver; ; epithelium of stomach; ; right kidney; ; decidua; ; human kidney; ; triceps brachii muscle;
	More reference expression data
	n/a
Gene ontology
Molecular function	molybdopterin cofactor binding; molybdenum ion binding; oxidoreductase activity; sulfite oxidase activity; heme binding; metal ion binding; protein binding;
Cellular component	mitochondrial matrix; mitochondrial intermembrane space; mitochondrion;
Biological process	sulfur compound metabolic process; sulfide oxidation, using sulfide:quinone oxidoreductase; nitrate assimilation;
	Sources:Amigo / QuickGO
Orthologs
	6821
	211389
	ENSG00000139531
	ENSMUSG00000049858
	P51687
	Q8R086
	NM_000456; NM_001032386; NM_001032387
	NM_173733
	NP_000447; NP_001027558; NP_001027559
	NP_776094
	Wikidata
View/Edit Human	View/Edit Mouse

Search
PMC	articles
PubMed	articles
NCBI	proteins

sulfite oxidase
sulfite oxidase
	Sulfite oxidase catalyses the oxidation-reduction reaction of sulfite and water, yielding sulfate.
Identifiers
EC no.	1.8.3.1
CAS no.	9029-38-3
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

Sulfite oxidase (EC 1.8.3.1) is an enzyme in the mitochondria of all eukaryotes, with exception of the yeasts.^{[citation needed]} It oxidizes sulfite to sulfate and, via cytochrome c, transfers the electrons produced to the electron transport chain, allowing generation of ATP in oxidative phosphorylation.^[5]^[6]^[7] This is the last step in the metabolism of sulfur-containing compounds and the sulfate is excreted.

Sulfite oxidase is a metallo-enzyme that utilizes a molybdopterin cofactor and a heme group (in the case of animals). It is one of the cytochromes b₅ and belongs to the enzyme super-family of molybdenum oxotransferases that also includes DMSO reductase, xanthine oxidase, and nitrite reductase.

In mammals, the expression levels of sulfite oxidase is high in the liver, kidney, and heart, and very low in spleen, brain, skeletal muscle, and blood.

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000139531 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000049858 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ D'Errico G, Di Salle A, La Cara F, Rossi M, Cannio R (January 2006). "Identification and characterization of a novel bacterial sulfite oxidase with no heme binding domain from Deinococcus radiodurans". J. Bacteriol. 188 (2): 694–701. doi:10.1128/JB.188.2.694-701.2006. PMC 1347283. PMID 16385059.
^ Tan WH, Eichler FS, Hoda S, Lee MS, Baris H, Hanley CA, Grant PE, Krishnamoorthy KS, Shih VE (September 2005). "Isolated sulfite oxidase deficiency: a case report with a novel mutation and review of the literature". Pediatrics. 116 (3): 757–66. doi:10.1542/peds.2004-1897. PMID 16140720. S2CID 6506338.
^ Cohen HJ, Betcher-Lange S, Kessler DL, Rajagopalan KV (December 1972). "Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity". J. Biol. Chem. 247 (23): 7759–66. doi:10.1016/S0021-9258(19)44588-2. PMID 4344230.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000139531 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000049858 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid16385059-5] D'Errico G, Di Salle A, La Cara F, Rossi M, Cannio R (January 2006). "Identification and characterization of a novel bacterial sulfite oxidase with no heme binding domain from Deinococcus radiodurans". J. Bacteriol. 188 (2): 694–701. doi:10.1128/JB.188.2.694-701.2006. PMC 1347283. PMID 16385059.

[pmid16140720-6] Tan WH, Eichler FS, Hoda S, Lee MS, Baris H, Hanley CA, Grant PE, Krishnamoorthy KS, Shih VE (September 2005). "Isolated sulfite oxidase deficiency: a case report with a novel mutation and review of the literature". Pediatrics. 116 (3): 757–66. doi:10.1542/peds.2004-1897. PMID 16140720. S2CID 6506338.

[pmid4344230-7] Cohen HJ, Betcher-Lange S, Kessler DL, Rajagopalan KV (December 1972). "Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity". J. Biol. Chem. 247 (23): 7759–66. doi:10.1016/S0021-9258(19)44588-2. PMID 4344230.

[1]

[2]

[3]

[4]

[5]

[6]

[7]