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Alcohol dehydrogenase (cytochrome c)
Alcohol dehydrogenase (cytochrome c)
Identifiers
EC no.	1.1.2.8
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

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

\rightleftharpoons

an aldehyde + 2 ferrocytochrome c + 2 H+

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

References

^ 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.
^ 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.
^ 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.
^ 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.
^ 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.
^ 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.