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an enzyme that catalyses the biochemical reduction of some specified substance

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2015/10/09 01:20:02」(JST)

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Sulfite reductases (EC 1.8.99.1) are important enzymes in the process of sulfur metabolism.^[2] They catalyze the reduction of sulfite to hydrogen sulfide and water.^[2]^[3] Electrons for the reaction are provided by a dissociable molecule of either NADPH, bound flavins, or ferredoxins.^[4]

SO₃²⁻ (sulfite) + electron donor H₂S (hydrogen sulfide) + oxidized donor + 3 H₂O

Sulfite reductases belong to the family of oxidoreductases, and are found in archaea, bacteria, fungi, and plants.^[5] They are grouped as either assimilatory or dissimilatory sulfite reductases depending on their function, their spectroscopic properties, and their catalytic properties. This enzyme participates in selenoamino acid metabolism and sulfur assimilation. It employs two covalently coupled cofactors - an iron sulfur cluster and a siroheme - which deliver electrons to the substrate via this coupling.^[6]

The systematic name of this enzyme class is hydrogen-sulfide:acceptor oxidoreductase. Other names in common use include assimilatory sulfite reductase, assimilatory-type sulfite reductase, and hydrogen-sulfide:(acceptor) oxidoreductase.

References

^ PDB: 1AOP; Crane BR, Siegel LM, Getzoff ED (October 1995). "Sulfite reductase structure at 1.6 Å: evolution and catalysis for reduction of inorganic anions". Science 270 (5233): 59–67. doi:10.1126/science.270.5233.59. PMID 7569952.
^ ^a ^b Parey K, Warkentin E, Kroneck PM, Ermler U (2010). "Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus". Biochemistry 49 (41): 8912–8921. doi:10.1021/bi100781f. PMID 20822098.
^ Pinto R, Harrison JS, Hsu T, Jacobs WR, Leyh TS (September 2007). "Sulfite Reduction in Mycobacteria". J. Bacteriol. 189 (18): 6714–22. doi:10.1128/JB.00487-07. PMC 2045171. PMID 17644602.
^ Siegel LM, Murphy MJ, Kamin H (January 1973). "Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups". J. Biol. Chem. 248 (1): 251–64. PMID 4144254.
^ Schnell R, Sandalova T, Hellman U, Lindqvist Y, Schneider G (July 2005). "Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site". J. Biol. Chem. 280 (29): 27319–28. doi:10.1074/jbc.M502560200. PMID 15917234.
^ Crane BR, Getzoff ED (December 1996). "The relationship between structure and function for the sulfite reductases". Curr. Opin. Struct. Biol. 6 (6): 744–56. doi:10.1016/S0959-440X(96)80003-0. PMID 8994874.

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English Journal

The role of extended Fe₄S₄ cluster ligands in mediating sulfite reductase hemoprotein activity.

Cepeda MR1, McGarry L2, Pennington JM2, Krzystek J3, Elizabeth Stroupe M2.
Biochimica et biophysica acta.Biochim Biophys Acta.2018 May 28. pii: S1570-9639(18)30080-3. doi: 10.1016/j.bbapap.2018.05.013. [Epub ahead of print]
PMID 29852252

Structure-Function Relationships in the Oligomeric NADPH-Dependent Assimilatory Sulfite Reductase.

Askenasy I, Murray D, Andrews RM, Uversky VN, He H, Stroupe ME.
Biochemistry.Biochemistry.2018 May 22. doi: 10.1021/acs.biochem.8b00446. [Epub ahead of print]
The central step in the assimilation of sulfur is a six-electron reduction of sulfite to sulfide, catalyzed by the oxidoreductase NADPH-dependent assimilatory Sulfite Reductase (SiR). SiR is composed of two subunits. One is a multi-domain flavin-binding reductase (SiRFP) and the other an iron-contai
PMID 29787249

Sulfur partitioning between glutathione and protein synthesis determines plant growth.

Speiser A1, Silbermann M1, Dong Y2, Haberland S1, Uslu VV3, Wang S1, Bangash SAK4, Reichelt M5, Meyer AJ6, Wirtz M7, Hell R8.
Plant physiology.Plant Physiol.2018 May 11. pii: pp.00421.2018. doi: 10.1104/pp.18.00421. [Epub ahead of print]
PMID 29752309

Japanese Journal

Kinetic Assays for Determining In Vitro APS Reductase Activity in Plants without the Use of Radioactive Substances

BRYCHKOVA Galina,YARMOLINSKY Dmitry,SAGI Moshe
Plant and cell physiology 53(9), 1648-1658, 2012-09-01
NAID 10031053664

Techniques : Kinetic Assays for Determining In Vitro APS Reductase Activity in Plants without the Use of Radioactive Substances

Brychkova Galina,Yarmolinsky Dmitry,Sagi Moshe
Plant and Cell Physiology 53(9), 1648-1658, 2012-09
NAID 40019417526

A Novel In-Gel Assay and an Improved Kinetic Assay for Determining In Vitro Sulfite Reductase Activity in Plants

BRYCHKOVA Galina,YARMOLINSKY Dmitry,VENTRUA Yvonne,SAGI Moshe
Plant and cell physiology 53(8), 1507-1516, 2012-08-01
NAID 10031052951

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★リンクテーブル★

リンク元	「亜硫酸還元酵素」「sulfite dehydrogenase」「sulfite oxidase」「亜硫酸レダクターゼ」
拡張検索	「hydrogensulfite reductase」「ferredoxin-dependent sulfite reductase」「NADPH-dependent sulfite reductase」
関連記事	「reductase」「sulfite」

「亜硫酸還元酵素」

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PMC	articles
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sulfite reductase
	Crystallographic structure of sulfite reductase from E. coli.
Identifiers
EC number	1.8.99.1
CAS number	37256-51-2
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 / EGO
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NCBI	proteins