Summary
We have traced the polypeptide chain at 3 Å resolution of the soluble, monomeric alcohol dehydrogenase (ADH-IIB) isolated from Pseudomonas putida. The enzyme contains a large N-terminal 8-stranded a-propeller domain (~60 kDa) similar to methanol dehydrogenase (MDH) and a small C-terminal c-type cytochrome domain (~ 10 kDa) similar to the cytochrome subunit of p-cresol methylhydoxylase (PCMH), also from P. putida. The heme is inclined by about 70º to the PQQ and their planes are about 14 Å apart at the closest point. The propionic acids of the heme group are exposed to solvent suggesting them to be the site for interaction with its azurin electron transfer partners.
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Reference
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Mathews, F.S., Chen, Zw., Toyama, H., Adachi, O., Bellamy, H.D. (2000). Structural Studies of a soluble monomeric Quinohemoprotein Alcohol Dehydrogenase from Pseudomonas putida HK5. In: Iriarte, A., Martinez-Carrion, M., Kagan, H.M. (eds) Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8397-9_35
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DOI: https://doi.org/10.1007/978-3-0348-8397-9_35
Publisher Name: Birkhäuser, Basel
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