Alcohol dehydrogenase (cytochrome c)

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Alcohol dehydrogenase (cytochrome c)
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EC no. 1.1.2.8
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Alcohol dehydrogenase (cytochrome c) (EC 1.1.2.8, type I quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase) is an enzyme with systematic name alcohol:cytochrome c oxidoreductase. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

a primary alcohol + 2 ferricytochrome c an aldehyde + 2 ferrocytochrome c + 2 H+

A periplasmic PQQ-containing quinoprotein is present in Pseudomonas and Rhodopseudomonas .

Related Research Articles

A dehydrogenase is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by reducing an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. Like all catalysts, they catalyze reverse as well as forward reactions, and in some cases this has physiological significance: for example, alcohol dehydrogenase catalyzes the oxidation of ethanol to acetaldehyde in animals, but in yeast it catalyzes the production of ethanol from acetaldehyde.

<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">Pyrroloquinoline quinone</span> Chemical compound

Pyrroloquinoline quinone (PQQ), also called methoxatin, is a redox cofactor and antioxidant. Produced by bacteria, it is found in soil and foods such as kiwifruit, as well as human breast milk. Enzymes using PQQ as a redox cofactor are called quinoproteins and play a variety of redox roles. Quinoprotein glucose dehydrogenase is used as a glucose sensor in bacteria. PQQ stimulates growth in bacteria. Eukaryote targets, including mammalian lactate dehydrogenase, are of more interest to health. It is suggested that PQQ taken as a dietary supplement could promote mitochondrial biogenesis via this pathway as well as PGC-1α.

<span class="mw-page-title-main">Pseudomonadaceae</span> Family of gram-negative bacteria

The Pseudomonadaceae are a family of bacteria which includes the genera Azomonas, Azorhizophilus, Azotobacter, Mesophilobacter, Pseudomonas, and Rugamonas. The family Azotobacteraceae was recently reclassified into this family.

The oxidase test is used to determine if an organism possesses the cytochrome c oxidase enzyme. The test is used as an aid for the differentiation of Neisseria, Moraxella, Campylobacter and Pasteurella species. It is also used to differentiate pseudomonads from related species.

<span class="mw-page-title-main">Carnitine 3-dehydrogenase</span>

In enzymology, a carnitine 3-dehydrogenase (EC 1.1.1.108) is an enzyme that catalyzes the chemical reaction

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

In enzymology, a methanol dehydrogenase (MDH) is an enzyme that catalyzes the chemical reaction:

In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction

In enzymology, a choline dehydrogenase is an enzyme that catalyzes the chemical reaction

In enzymology, a polyvinyl-alcohol dehydrogenase (acceptor) is an enzyme that catalyzes the chemical reaction

In enzymology, a quinoprotein glucose dehydrogenase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Nitrite reductase (NO-forming)</span> Class of enzymes

In enzymology, a nitrite reductase (NO-forming) (EC 1.7.2.1) is an enzyme that catalyzes the chemical reaction

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

Thiosulfate dehydrogenase is an enzyme that catalyzes the chemical reaction:

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

Azurin is a small, periplasmic, bacterial blue copper protein found in Pseudomonas, Bordetella, or Alcaligenes bacteria. Azurin moderates single-electron transfer between enzymes associated with the cytochrome chain by undergoing oxidation-reduction between Cu(I) and Cu(II). Each monomer of an azurin tetramer has a molecular weight of approximately 14kDa, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308 nm.

Polyvinyl alcohol dehydrogenase (cytochrome) (EC 1.1.2.6, PVA dehydrogenase, PVADH) is an enzyme with systematic name polyvinyl alcohol:ferricytochrome-c oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Methanol dehydrogenase (cytochrome c)</span>

Methanol dehydrogenase (cytochrome c) (EC 1.1.2.7, methanol dehydrogenase, MDH) is an enzyme with systematic name methanol:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction

Alcohol dehydrogenase (quinone) (EC 1.1.5.5, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an enzyme with systematic name alcohol:quinone oxidoreductase. This enzyme catalyses the following chemical reaction

Alcohol dehydrogenase (azurin) (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB) is an enzyme with systematic name alcohol:azurin oxidoreductase. This enzyme catalyses the following chemical reaction

Soluble quinoprotein glucose dehydrogenase is an enzyme with systematic name D-glucose:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction

Lupanine 17-hydroxylase (cytochrome c) (EC 1.17.2.2, lupanine dehydrogenase (cytochrome c)) is an enzyme with systematic name lupanine:cytochrome c-oxidoreductase (17-hydroxylating). This enzyme catalyses the following chemical reaction

References

  1. Rupp M, Görisch H (June 1988). "Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa". Biological Chemistry Hoppe-Seyler. 369 (6): 431–9. doi:10.1515/bchm3.1988.369.1.431. PMID   3144289.
  2. Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O (May 1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". Journal of Bacteriology. 177 (9): 2442–50. doi:10.1128/jb.177.9.2442-2450.1995. PMC   176903 . PMID   7730276.
  3. Schobert M, Görisch H (February 1999). "Cytochrome c550 is an essential component of the quinoprotein ethanol oxidation system in Pseudomonas aeruginosa: cloning and sequencing of the genes encoding cytochrome c550 and an adjacent acetaldehyde dehydrogenase". Microbiology. 145 ( Pt 2): 471–81. doi: 10.1099/13500872-145-2-471 . PMID   10075429.
  4. Keitel T, Diehl A, Knaute T, Stezowski JJ, Höhne W, Görisch H (April 2000). "X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity". Journal of Molecular Biology. 297 (4): 961–74. doi:10.1006/jmbi.2000.3603. PMID   10736230.
  5. Kay CW, Mennenga B, Görisch H, Bittl R (April 2004). "Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy". FEBS Letters. 564 (1–2): 69–72. doi: 10.1016/S0014-5793(04)00317-5 . PMID   15094044.
  6. Mennenga B, Kay CW, Görisch H (April 2009). "Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550". Archives of Microbiology. 191 (4): 361–7. doi:10.1007/s00203-009-0460-4. PMID   19224199.