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{{Infobox enzyme
| 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 system name ''alcohol:cytochrome c oxidoreductase''.<ref>{{cite journal | title = Purification, crystallisation and characterization of quinoprotein ethanol dehydrogenase from ''Pseudomonas aeruginosa'' |author = Rupp, M. and Gorisch, H. |journal = Biol. Chem. Hoppe-Seyler |year = 1988 |volume = 369 |pages = 431–439 |pmid = 3144289 |issue=6}}</ref><ref>{{cite journal | title = Three distinct quinoprotein alcohol dehydrogenases are expressed when ''Pseudomonas putida'' is grown on different alcohols |author = Toyama, H., Fujii, A., Matsushita, K., Shinagawa, E., Ameyama, M. and Adachi, O. |journal = J. Bacteriol. |year = 1995 |volume = 177 |pages = 2442–2450 |pmid = 7730276 |pmc=176903 |issue=9}}</ref><ref>{{cite journal | title = Cytochrome ''c''<sub>550</sub> is an essential component of the quinoprotein ethanol oxidation system in ''Pseudomonas aeruginosa'': cloning and sequencing of the genes encoding cytochrome ''c''<sub>550</sub> and an adjacent acetaldehyde dehydrogenase |author = Schobert, M. and Gorisch, H. |journal = Microbiology |year = 1999 |volume = 145 |pages = 471–481 |pmid = 10075429}}</ref><ref>{{cite journal | title = X-ray structure of the quinoprotein ethanol dehydrogenase from ''Pseudomonas aeruginosa'': basis of substrate specificity |author = Keitel, T., Diehl, A., Knaute, T., Stezowski, J.J., Hohne, W. and Gorisch, H. |journal = J. Mol. Biol. |year = 2000 |volume = 297 |pages = 961–974 |pmid = 10736230 |doi=10.1006/jmbi.2000.3603 |issue=4}}</ref><ref>{{cite journal | title = Characterisation of the PQQ cofactor radical in quinoprotein ethanol dehydrogenase of ''Pseudomonas aeruginosa'' by electron paramagnetic resonance  spectroscopy |author = Kay, C.W., Mennenga, B., Gorisch, H. and 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}}</ref><ref>{{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 ''c''<sub>550</sub> |author = Mennenga, B., Kay, C.W. and Gorisch, H. |journal = Arch. Microbiol. |year = 2009 |volume = 191 |pages = 361–367 |pmid = 19224199 |doi=10.1007/s00203-009-0460-4 |issue=4}}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]]

: a primary alcohol + 2 ferricytochrome c <math>\rightleftharpoons</math> an aldehyde + 2 ferrocytochrome c + 2 H+

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

== References ==
{{reflist}}

== External links ==
* {{MeshName|Alcohol+dehydrogenase+(cytochrome+c)}}

[[Category:EC 1.1.2]]