Sulfite reductase

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sulfite reductase
1aop SulfiteReductase.jpg
Crystallographic structure of sulfite reductase from E. coli . [1]
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EC no. 1.8.99.1
CAS no. 37256-51-2
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Sulfite reductases (EC 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 donor H2S (hydrogen sulfide) + oxidized donor + 3 H2O

Sulfite reductases, which belong to the oxidoreductase family, are found in the archaea, bacteria, fungi, and plants. [5] [6] [7] They are grouped as either the assimilatory or the 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 the 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.

Related Research Articles

Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.

<span class="mw-page-title-main">Sulfate-reducing microorganism</span> Microorganisms that "breathe" sulfates

Sulfate-reducing microorganisms (SRM) or sulfate-reducing prokaryotes (SRP) are a group composed of sulfate-reducing bacteria (SRB) and sulfate-reducing archaea (SRA), both of which can perform anaerobic respiration utilizing sulfate (SO2−
4
) as terminal electron acceptor, reducing it to hydrogen sulfide (H2S). Therefore, these sulfidogenic microorganisms "breathe" sulfate rather than molecular oxygen (O2), which is the terminal electron acceptor reduced to water (H2O) in aerobic respiration.

Nitrite reductase refers to any of several classes of enzymes that catalyze the reduction of nitrite. There are two classes of NIR's. A multi haem enzyme reduces NO2 to a variety of products. Copper containing enzymes carry out a single electron transfer to produce nitric oxide.

Microbial metabolism is the means by which a microbe obtains the energy and nutrients it needs to live and reproduce. Microbes use many different types of metabolic strategies and species can often be differentiated from each other based on metabolic characteristics. The specific metabolic properties of a microbe are the major factors in determining that microbe's ecological niche, and often allow for that microbe to be useful in industrial processes or responsible for biogeochemical cycles.

In enzymology, a sulfhydrogenase, also known as sulfur reductase, is an enzyme that catalyzes the reduction of elemental sulfur or polysulfide to hydrogen sulfide using hydrogen as electron donor.

<span class="mw-page-title-main">Adenylyl-sulfate reductase</span> Class of enzymes

Adenylyl-sulfate reductase is an enzyme that catalyzes the chemical reaction of the reduction of adenylyl-sulfate/adenosine-5'-phosphosulfate (APS) to sulfite through the use of an electron donor cofactor. The products of the reaction are AMP and sulfite, as well as an oxidized electron donor cofactor.

Adenylyl-sulfate reductase (glutathione) is an enzyme that catalyzes the chemical reaction

Adenylyl-sulfate reductase (thioredoxin) is an enzyme that catalyzes the chemical reaction

In enzymology, a ferredoxin—nitrate reductase (EC 1.7.7.2) is an enzyme that catalyzes the chemical reaction

In enzymology, a hydrogensulfite reductase (EC 1.8.99.3) is an enzyme that catalyzes the chemical reaction

In enzymology, a nitrite reductase [NAD(P)H] (EC 1.7.1.4) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Sulfite reductase (NADPH)</span>

Sulfite reductase (NADPH) (EC 1.8.1.2, sulfite (reduced nicotinamide adenine dinucleotide phosphate) reductase, NADPH-sulfite reductase, NADPH-dependent sulfite reductase, H2S-NADP oxidoreductase, sulfite reductase (NADPH2)) is an enzyme with systematic name hydrogen-sulfide:NADP+ oxidoreductase. This enzyme catalises the following chemical reaction

Sulfur is metabolized by all organisms, from bacteria and archaea to plants and animals. Sulfur can have an oxidation state from -2 to +6 and is reduced or oxidized by a diverse range of organisms. The element is present in proteins, sulfate esters of polysaccharides, steroids, phenols, and sulfur-containing coenzymes.

<span class="mw-page-title-main">Siroheme</span>

Siroheme is a heme-like prosthetic group at the active sites of some enzymes to accomplish the six-electron reduction of sulfur and nitrogen. It is a cofactor at the active site of sulfite reductase, which plays a major role in sulfur assimilation pathway, converting sulfite into sulfide, which can be incorporated into the organic compound homocysteine.

<span class="mw-page-title-main">Short-chain acyl-CoA dehydrogenase</span>

Short-chain acyl-CoA dehydrogenase is an enzyme with systematic name short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

Sulfide:quinone reductase is an enzyme with systematic name sulfide:quinone oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Dissimilatory sulfate reduction</span> Form of anaerobic respiration where sulfate is the terminal electron acceptor

Dissimilatory sulfate reduction is a form of anaerobic respiration that uses sulfate as the terminal electron acceptor to produce hydrogen sulfide. This metabolism is found in some types of bacteria and archaea which are often termed sulfate-reducing organisms. The term "dissimilatory" is used when hydrogen sulfide is produced in an anaerobic respiration process. By contrast, the term "assimilatory" would be used in relation to the biosynthesis of organosulfur compounds, even though hydrogen sulfide may be an intermediate.

<span class="mw-page-title-main">Aldehyde ferredoxin oxidoreductase</span>

In enzymology, an aldehyde ferredoxin oxidoreductase (EC 1.2.7.5) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Microbial oxidation of sulfur</span>

Microbial oxidation of sulfur is the oxidation of sulfur by microorganisms to build their structural components. The oxidation of inorganic compounds is the strategy primarily used by chemolithotrophic microorganisms to obtain energy to survive, grow and reproduce. Some inorganic forms of reduced sulfur, mainly sulfide (H2S/HS) and elemental sulfur (S0), can be oxidized by chemolithotrophic sulfur-oxidizing prokaryotes, usually coupled to the reduction of oxygen (O2) or nitrate (NO3). Anaerobic sulfur oxidizers include photolithoautotrophs that obtain their energy from sunlight, hydrogen from sulfide, and carbon from carbon dioxide (CO2).

Dissimilatory sulfite reductase is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction.

References

  1. PDB: 1AOP ; Crane BR, Siegel LM, Getzoff ED (October 1995). "Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions". Science. 270 (5233): 59–67. Bibcode:1995Sci...270...59C. doi:10.1126/science.270.5233.59. PMID   7569952. S2CID   31246227.
  2. 1 2 Parey K, Warkentin E, Kroneck PM, Ermler U (October 2010). "Reaction cycle of the dissimilatory sulfite reductase from Archaeoglobus fulgidus". Biochemistry. 49 (41): 8912–21. doi:10.1021/bi100781f. PMID   20822098.
  3. Pinto R, Harrison JS, Hsu T, Jacobs WR, Leyh TS (September 2007). "Sulfite reduction in mycobacteria". Journal of Bacteriology. 189 (18): 6714–22. doi:10.1128/JB.00487-07. PMC   2045171 . PMID   17644602.
  4. 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". The Journal of Biological Chemistry. 248 (1): 251–64. doi: 10.1016/S0021-9258(19)44469-4 . PMID   4144254.
  5. Brychkova G, Yarmolinsky D, Ventura Y, Sagi M (August 2012). "A novel in-gel assay and an improved kinetic assay for determining in vitro sulfite reductase activity in plants". Plant & Cell Physiology. 53 (8): 1507–16. doi: 10.1093/pcp/pcs084 . PMID   22685081.
  6. Yarmolinsky D, Brychkova G, Kurmanbayeva A, Bekturova A, Ventura Y, Khozin-Goldberg I, Eppel A, Fluhr R, Sagi M (August 2014). "Impairment in Sulfite Reductase Leads to Early Leaf Senescence in Tomato Plants". Plant Physiology. 165 (4): 1505–1520. doi:10.1104/pp.114.241356. PMC   4119034 . PMID   24987017.
  7. 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". The Journal of Biological Chemistry. 280 (29): 27319–28. doi: 10.1074/jbc.M502560200 . PMID   15917234.
  8. Crane BR, Getzoff ED (December 1996). "The relationship between structure and function for the sulfite reductases". Current Opinion in Structural Biology. 6 (6): 744–56. doi:10.1016/S0959-440X(96)80003-0. PMID   8994874.

Further reading