- References
- Further reading
| Name = sulfite reductase
| EC_number = 1.8.99.1
| CAS_number = 37256-51-2
| IUBMB_EC_number = 1/8/99/1
| GO_code = 0016002
| PDB =1AOP, 8GEP
| image = 1aop_SulfiteReductase.jpg
| width =
| caption = Crystallographic structure of sulfite reductase from E. coli.[1]
}}Sulfite reductases ({{EC number|1.8.99.1}}) are enzymes that participate in 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 donorH2S (hydrogen sulfide) + oxidized donor + 3 H2O
Sulfite reductases, which belong to the oxidoreductase family, are found in archaea, bacteria, fungi, and plants[5][6][7]. 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.[8]
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
1. ^{{PDB|1AOP}}; {{cite journal | vauthors = Crane BR, Siegel LM, Getzoff ED | title = Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions | journal = Science | volume = 270 | issue = 5233 | pages = 59–67 | date = October 1995 | pmid = 7569952 | doi = 10.1126/science.270.5233.59 }}
2. ^1 {{cite journal | vauthors = Parey K, Warkentin E, Kroneck PM, Ermler U | title = Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus | journal = Biochemistry | volume = 49 | issue = 41 | pages = 8912–21 | date = October 2010 | pmid = 20822098 | doi = 10.1021/bi100781f }}
3. ^{{cite journal | vauthors = Pinto R, Harrison JS, Hsu T, Jacobs WR, Leyh TS | title = Sulfite reduction in mycobacteria | journal = Journal of Bacteriology | volume = 189 | issue = 18 | pages = 6714–22 | date = September 2007 | pmid = 17644602 | pmc = 2045171 | doi = 10.1128/JB.00487-07 }}
4. ^{{cite journal | vauthors = Siegel LM, Murphy MJ, Kamin H | title = Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups | journal = The Journal of Biological Chemistry | volume = 248 | issue = 1 | pages = 251–64 | date = January 1973 | pmid = 4144254 | doi = }}
5. ^{{cite journal | vauthors = Brychkova G, Yarmolinsky D, Ventura Y, Sagi M | title = A novel in-gel assay and an improved kinetic assay for determining in vitro sulfite reductase activity in plants | journal = Plant & Cell Physiology | volume = 53 | issue = 8 | pages = 1507–16 | date = August 2012 | pmid = 22685081 | doi = 10.1093/pcp/pcs084 }}
6. ^{{cite journal | vauthors = Yarmolinsky D, Brychkova G, Kurmanbayeva A, Bekturova A, Ventura Y, Khozin-Goldberg I, Eppel A, Fluhr R, Sagi M | title = Impairment in Sulfite Reductase Leads to Early Leaf Senescence in Tomato Plants | journal = Plant Physiology | volume = 165 | issue = 4 | pages = 1505–1520 | date = August 2014 | pmid = 24987017 | pmc = 4119034 | doi = 10.1104/pp.114.241356 }}
7. ^{{cite journal | vauthors = Schnell R, Sandalova T, Hellman U, Lindqvist Y, Schneider G | title = Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site | journal = The Journal of Biological Chemistry | volume = 280 | issue = 29 | pages = 27319–28 | date = July 2005 | pmid = 15917234 | doi = 10.1074/jbc.M502560200 }}
8. ^{{cite journal | vauthors = Crane BR, Getzoff ED | title = The relationship between structure and function for the sulfite reductases | journal = Current Opinion in Structural Biology | volume = 6 | issue = 6 | pages = 744–56 | date = December 1996 | pmid = 8994874 | doi = 10.1016/S0959-440X(96)80003-0 }}
2. ^1 {{cite journal | vauthors = Parey K, Warkentin E, Kroneck PM, Ermler U | title = Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus | journal = Biochemistry | volume = 49 | issue = 41 | pages = 8912–21 | date = October 2010 | pmid = 20822098 | doi = 10.1021/bi100781f }}
3. ^{{cite journal | vauthors = Pinto R, Harrison JS, Hsu T, Jacobs WR, Leyh TS | title = Sulfite reduction in mycobacteria | journal = Journal of Bacteriology | volume = 189 | issue = 18 | pages = 6714–22 | date = September 2007 | pmid = 17644602 | pmc = 2045171 | doi = 10.1128/JB.00487-07 }}
4. ^{{cite journal | vauthors = Siegel LM, Murphy MJ, Kamin H | title = Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups | journal = The Journal of Biological Chemistry | volume = 248 | issue = 1 | pages = 251–64 | date = January 1973 | pmid = 4144254 | doi = }}
5. ^{{cite journal | vauthors = Brychkova G, Yarmolinsky D, Ventura Y, Sagi M | title = A novel in-gel assay and an improved kinetic assay for determining in vitro sulfite reductase activity in plants | journal = Plant & Cell Physiology | volume = 53 | issue = 8 | pages = 1507–16 | date = August 2012 | pmid = 22685081 | doi = 10.1093/pcp/pcs084 }}
6. ^{{cite journal | vauthors = Yarmolinsky D, Brychkova G, Kurmanbayeva A, Bekturova A, Ventura Y, Khozin-Goldberg I, Eppel A, Fluhr R, Sagi M | title = Impairment in Sulfite Reductase Leads to Early Leaf Senescence in Tomato Plants | journal = Plant Physiology | volume = 165 | issue = 4 | pages = 1505–1520 | date = August 2014 | pmid = 24987017 | pmc = 4119034 | doi = 10.1104/pp.114.241356 }}
7. ^{{cite journal | vauthors = Schnell R, Sandalova T, Hellman U, Lindqvist Y, Schneider G | title = Siroheme- and [Fe4-S4]-dependent NirA from Mycobacterium tuberculosis is a sulfite reductase with a covalent Cys-Tyr bond in the active site | journal = The Journal of Biological Chemistry | volume = 280 | issue = 29 | pages = 27319–28 | date = July 2005 | pmid = 15917234 | doi = 10.1074/jbc.M502560200 }}
8. ^{{cite journal | vauthors = Crane BR, Getzoff ED | title = The relationship between structure and function for the sulfite reductases | journal = Current Opinion in Structural Biology | volume = 6 | issue = 6 | pages = 744–56 | date = December 1996 | pmid = 8994874 | doi = 10.1016/S0959-440X(96)80003-0 }}
Further reading
{{refbegin}}- {{cite journal | vauthors = Asada K | title = Purification and properties of a sulfite reductase from leaf tissue | journal = The Journal of Biological Chemistry | volume = 242 | issue = 16 | pages = 3646–54 | date = August 1967 | pmid = 6038492 | doi = }}
- {{cite journal | vauthors = Asada K, Tamura G, Bandurski RS | title = Methyl viologen-linked sulfite reductase from spinach leaves | journal = The Journal of Biological Chemistry | volume = 244 | issue = 18 | pages = 4904–15 | date = September 1969 | pmid = 5824566 | doi = }}
- {{cite journal | vauthors = Yoshimoto A, Nakamura T, Sato R | title = Isolation from Aspergillus nidulans, of a protein catalyzing the reduction of sulfite by reduced viologen dyes | journal = Journal of Biochemistry | volume = 62 | issue = 6 | pages = 756–66 | date = December 1967 | pmid = 5589532 | doi = 10.1093/oxfordjournals.jbchem.a128732}}
3 : EC 1.8.99|Iron enzymes|Sulfur metabolism
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