Nitrate reductase (quinone)

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Nitrate reductase (quinone)
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EC no. 1.7.5.1
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Nitrate reductase (quinone) (EC 1.7.5.1, nitrate reductase A, nitrate reductase Z, quinol/nitrate oxidoreductase, quinol-nitrate oxidoreductase, quinol:nitrate oxidoreductase, NarA, NarZ, NarGHI) is an enzyme with systematic name nitrite:quinone oxidoreductase. [1] [2] [3] [4] [5] [6] [7] This enzyme catalyses the following chemical reaction

nitrate + a quinol nitrite + a quinone + H2O

This is a membrane-bound enzyme which supports [anaerobic respiration] on nitrate.

Related Research Articles

<span class="mw-page-title-main">Electron transport chain</span> Energy-producing metabolic pathway

An electron transport chain (ETC) is a series of protein complexes and other molecules that transfer electrons from electron donors to electron acceptors via redox reactions (both reduction and oxidation occurring simultaneously) and couples this electron transfer with the transfer of protons (H+ ions) across a membrane. The electrons that are transferred from NADH and FADH2 to the ETC involves four multi-subunit large enzymes complexes and two mobile electron carriers. Many of the enzymes in the electron transport chain are embedded within the membrane.

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

Nitrate reductases are molybdoenzymes that reduce nitrate to nitrite. This reaction is critical for the production of protein in most crop plants, as nitrate is the predominant source of nitrogen in fertilized soils.

Nitrate reductase (NADH) (EC 1.7.1.1, assimilatory nitrate reductase, NADH-nitrate reductase, NADH-dependent nitrate reductase, assimilatory NADH: nitrate reductase, nitrate reductase (NADH2), NADH2:nitrate oxidoreductase) is an enzyme with systematic name nitrite:NAD+ oxidoreductase. This enzyme catalyzes the following chemical reaction

In enzymology, a hydrogen:quinone oxidoreductase (EC 1.12.5.1) is an enzyme that catalyzes the chemical reaction

In enzymology, an FMN reductase (EC 1.5.1.29) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">NAD(P)H dehydrogenase (quinone)</span>

In enzymology, a NAD(P)H dehydrogenase (quinone) (EC 1.6.5.2) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Cytochrome c nitrite reductase</span> Class of enzymes

Cytochrome c nitrite reductase (ccNiR) is a bacterial enzyme that catalyzes the six electron reduction of nitrite to ammonia; an important step in the biological nitrogen cycle. The enzyme catalyses the second step in the two step conversion of nitrate to ammonia, which allows certain bacteria to use nitrite as a terminal electron acceptor, rather than oxygen, during anaerobic conditions. During this process, ccNiR draws electrons from the quinol pool, which are ultimately provided by a dehydrogenase such as formate dehydrogenase or hydrogenase. These dehydrogenases are responsible for generating a proton motive force.

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

The fnr gene of Escherichia coli encodes a transcriptional activator (FNR) which is required for the expression of a number of genes involved in anaerobic respiratory pathways. The FNR protein of E. coli is an oxygen – responsive transcriptional regulator required for the switch from aerobic to anaerobic metabolism.

"Type III mutants, originally frdB, were designated fnr because they were defective in fumarate and nitrate reduction and impaired in their ability to produce gas." - Lambden and Guest, 1976 Journal of General Microbiology97, 145-160

<span class="mw-page-title-main">Diacetyl reductase ((S)-acetoin forming)</span>

Diacetyl reductase ((S)-acetoin forming) (EC 1.1.1.304, (S)-acetoin dehydrogenase) is an enzyme with systematic name (S)-acetoin:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Glycerol-3-phosphate dehydrogenase (quinone)</span>

Glycerol-3-phosphate dehydrogenase (EC 1.1.5.3 is an enzyme with systematic name sn-glycerol 3-phosphate:quinone oxidoreductase. This enzyme catalyses the following chemical reaction

Formate dehydrogenase-N (EC 1.1.5.6, Fdh-N, FdnGHI, nitrate-inducible formate dehydrogenase, formate dehydrogenase N, FDH-N, nitrate inducible Fdn, nitrate inducible formate dehydrogenase) is an enzyme with systematic name formate:quinone oxidoreductase. This enzyme catalyses the following chemical reaction

Crotonyl-CoA reductase (EC 1.3.1.86, butyryl-CoA dehydrogenase, butyryl dehydrogenase, unsaturated acyl-CoA reductase, ethylene reductase, enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, CCR) is an enzyme with systematic name butanoyl-CoA:NADP+ 2,3-oxidoreductase. This enzyme catalyses the following chemical reaction

Acrylyl-CoA reductase (NADH) (EC 1.3.1.95) is an enzyme with systematic name propanoyl-CoA:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Fumarate reductase (quinol)</span>

Fumarate reductase (quinol) (EC 1.3.5.4, QFR,FRD, menaquinol-fumarate oxidoreductase, quinol:fumarate reductase) is an enzyme with systematic name succinate:quinone oxidoreductase. This enzyme catalyzes the following chemical reaction:

9,9'-dicis-zeta-carotene desaturase is an enzyme with systematic name 9,9'-dicis-zeta-corotene:quinone oxidoreductase. This enzyme catalyses the following chemical reaction

FMN reductase (NADPH) (EC 1.5.1.38, FRP, flavin reductase P, SsuE) is an enzyme with systematic name FMNH2:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction:

<span class="mw-page-title-main">NADH:ubiquinone reductase (non-electrogenic)</span> Class of enzymes

NADH:ubiquinone reductase (non-electrogenic) (EC 1.6.5.9, NDH-2, ubiquinone reductase, coenzyme Q reductase, dihydronicotinamide adenine dinucleotide-coenzyme Q reductase, DPNH-coenzyme Q reductase, DPNH-ubiquinone reductase, NADH-coenzyme Q oxidoreductase, NADH-coenzyme Q reductase, NADH-CoQ oxidoreductase, NADH-CoQ reductase) is an enzyme with systematic name NADH:ubiquinone 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">Athel Cornish-Bowden</span> British biochemist

Athel Cornish-Bowden is a British biochemist known for his numerous textbooks, particularly those on enzyme kinetics and his work on metabolic control analysis.

References

  1. ↑ Enoch HG, Lester RL (December 1974). "The role of a novel cytochrome b-containing nitrate reductase and quinone in the in vitro reconstruction of formate-nitrate reductase activity of E. coli". Biochemical and Biophysical Research Communications. 61 (4): 1234–41. doi:10.1016/s0006-291x(74)80416-x. PMID   4616697.
  2. ↑ Bertero MG, Rothery RA, Palak M, Hou C, Lim D, Blasco F, Weiner JH, Strynadka NC (September 2003). "Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A". Nature Structural Biology. 10 (9): 681–7. doi:10.1038/nsb969. PMID   12910261.
  3. ↑ Lanciano P, Magalon A, Bertrand P, Guigliarelli B, Grimaldi S (May 2007). "High-stability semiquinone intermediate in nitrate reductase A (NarGHI) from Escherichia coli is located in a quinol oxidation site close to heme bD". Biochemistry. 46 (18): 5323–9. doi:10.1021/bi700074y. PMID   17439244.
  4. ↑ Bertero MG, Rothery RA, Boroumand N, Palak M, Blasco F, Ginet N, Weiner JH, Strynadka NC (April 2005). "Structural and biochemical characterization of a quinol binding site of Escherichia coli nitrate reductase A". The Journal of Biological Chemistry. 280 (15): 14836–43. doi: 10.1074/jbc.M410457200 . PMID   15615728.
  5. ↑ Bonnefoy V, Demoss JA (1994). "Nitrate reductases in Escherichia coli". Antonie van Leeuwenhoek. 66 (1–3): 47–56. doi:10.1007/bf00871632. PMID   7747940.
  6. ↑ Guigliarelli B, Asso M, More C, Augier V, Blasco F, Pommier J, Giordano G, Bertrand P (July 1992). "EPR and redox characterization of iron-sulfur centers in nitrate reductases A and Z from Escherichia coli. Evidence for a high-potential and a low-potential class and their relevance in the electron-transfer mechanism". European Journal of Biochemistry. 207 (1): 61–8. doi: 10.1111/j.1432-1033.1992.tb17020.x . PMID   1321049.
  7. ↑ Iobbi-Nivol C, Santini CL, Blasco F, Giordano G (March 1990). "Purification and further characterization of the second nitrate reductase of Escherichia coli K12". European Journal of Biochemistry. 188 (3): 679–87. doi: 10.1111/j.1432-1033.1990.tb15450.x . PMID   2139607.
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