Alcohol dehydrogenase (cytochrome c)
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.
References
- ↑ Rupp, M. and Gorisch, H. (1988). "Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa". Biol. Chem. Hoppe-Seyler 369 (6): 431–439. doi:10.1515/bchm3.1988.369.1.431. PMID 3144289.
- ↑ Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. (1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". J. Bacteriol. 177 (9): 2442–2450. PMC 176903. PMID 7730276.
- ↑ Schobert, M. and Gorisch, H. (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: 471–481. doi:10.1099/13500872-145-2-471. PMID 10075429.
- ↑ Keitel, T., Diehl, A., Knaute, T., Stezowski, J.J., Hohne, W. and Gorisch, H. (2000). "X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity". J. Mol. Biol. 297 (4): 961–974. doi:10.1006/jmbi.2000.3603. PMID 10736230.
- ↑ Kay, C.W., Mennenga, B., Gorisch, H. and Bittl, R. (2004). "Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy". FEBS Lett. 564 (1-2): 69–72. doi:10.1016/S0014-5793(04)00317-5. PMID 15094044.
- ↑ Mennenga, B., Kay, C.W. and Gorisch, H. (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". Arch. Microbiol. 191 (4): 361–367. doi:10.1007/s00203-009-0460-4. PMID 19224199.
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