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| Name = Alcohol dehydrogenase (cytochrome c)
| EC_number = 1.1.2.8
| CAS_number =
| IUBMB_EC_number = 1/1/2/8
| GO_code =
| image =
| width =
| caption =
}}Alcohol dehydrogenase (cytochrome c) ({{EC number|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 can aldehyde + 2 ferrocytochrome c + 2 H+
A periplasmic PQQ-containing quinoprotein is present in Pseudomonas and Rhodopseudomonas.
References
1. ^{{cite journal | title = Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa |author1 = Rupp, M. |author2 =Gorisch, H. |journal = Biol. Chem. Hoppe-Seyler |year = 1988 |volume = 369 |pages = 431–439 |pmid = 3144289 |issue=6 |doi=10.1515/bchm3.1988.369.1.431}}
2. ^{{cite journal | title = Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols |author1 = Toyama, H. |author2 =Fujii, A. |author3 =Matsushita, K. |author4 =Shinagawa, E. |author5 =Ameyama, M. |author6 =Adachi, O. | journal = J. Bacteriol. |year = 1995 |volume = 177 |pages = 2442–2450 |pmid = 7730276 |pmc=176903 |issue=9}}
3. ^{{cite journal | title = 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 |author1 = Schobert, M. |author2 =Gorisch, H. |journal = Microbiology |year = 1999 |volume = 145 |pages = 471–481 |pmid = 10075429 |doi=10.1099/13500872-145-2-471}}
4. ^{{cite journal | title = X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity |author1 = Keitel, T. |author2 =Diehl, A. |author3 =Knaute, T. |author4 =Stezowski, J.J. |author5 =Hohne, W. |author6 =Gorisch, H. | journal = J. Mol. Biol. |year = 2000 |volume = 297 |pages = 961–974 |pmid = 10736230 |doi=10.1006/jmbi.2000.3603 |issue=4}}
5. ^{{cite journal | title = Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy |author1 = Kay, C.W. |author2 =Mennenga, B. |author3 =Gorisch, H. |author4 =Bittl, R. |journal = FEBS Lett. |year = 2004 |volume = 564 |pages = 69–72 |pmid = 15094044 |doi=10.1016/S0014-5793(04)00317-5 |issue=1-2}}
6. ^{{cite journal | title = Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550 |author1 = Mennenga, B. |author2 =Kay, C.W. |author3 =Gorisch, H. |journal = Arch. Microbiol. |year = 2009 |volume = 191 |pages = 361–367 |pmid = 19224199 |doi=10.1007/s00203-009-0460-4 |issue=4}}
2. ^{{cite journal | title = Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols |author1 = Toyama, H. |author2 =Fujii, A. |author3 =Matsushita, K. |author4 =Shinagawa, E. |author5 =Ameyama, M. |author6 =Adachi, O. | journal = J. Bacteriol. |year = 1995 |volume = 177 |pages = 2442–2450 |pmid = 7730276 |pmc=176903 |issue=9}}
3. ^{{cite journal | title = 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 |author1 = Schobert, M. |author2 =Gorisch, H. |journal = Microbiology |year = 1999 |volume = 145 |pages = 471–481 |pmid = 10075429 |doi=10.1099/13500872-145-2-471}}
4. ^{{cite journal | title = X-ray structure of the quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: basis of substrate specificity |author1 = Keitel, T. |author2 =Diehl, A. |author3 =Knaute, T. |author4 =Stezowski, J.J. |author5 =Hohne, W. |author6 =Gorisch, H. | journal = J. Mol. Biol. |year = 2000 |volume = 297 |pages = 961–974 |pmid = 10736230 |doi=10.1006/jmbi.2000.3603 |issue=4}}
5. ^{{cite journal | title = Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of Pseudomonas aeruginosa by electron paramagnetic resonance spectroscopy |author1 = Kay, C.W. |author2 =Mennenga, B. |author3 =Gorisch, H. |author4 =Bittl, R. |journal = FEBS Lett. |year = 2004 |volume = 564 |pages = 69–72 |pmid = 15094044 |doi=10.1016/S0014-5793(04)00317-5 |issue=1-2}}
6. ^{{cite journal | title = Quinoprotein ethanol dehydrogenase from Pseudomonas aeruginosa: the unusual disulfide ring formed by adjacent cysteine residues is essential for efficient electron transfer to cytochrome c550 |author1 = Mennenga, B. |author2 =Kay, C.W. |author3 =Gorisch, H. |journal = Arch. Microbiol. |year = 2009 |volume = 191 |pages = 361–367 |pmid = 19224199 |doi=10.1007/s00203-009-0460-4 |issue=4}}
External links
- {{MeshName|Alcohol+dehydrogenase+(cytochrome+c)}}
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