Furfural reduction mechanism of a zinc-dependent alcohol dehydrogenase from Cupriavidus necator JMP134
| Autor: | Travis Hooper, Robert P. Hayes, Mark S. Nissen, ChulHee Kang, Qunrui Li, Luying Xun, Emiliano J. Sanchez, Brian N. Webb |
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| Rok vydání: | 2011 |
| Předmět: |
chemistry.chemical_classification
Ethanol integumentary system biology Stereochemistry Cupriavidus necator Furfural biology.organism_classification Microbiology Cofactor chemistry.chemical_compound Glycerol-3-phosphate dehydrogenase chemistry Biochemistry Oxidoreductase biology.protein NAD+ kinase Molecular Biology Alcohol dehydrogenase |
| Zdroj: | Molecular Microbiology. 83:85-95 |
| ISSN: | 0950-382X |
| DOI: | 10.1111/j.1365-2958.2011.07914.x |
| Popis: | Summary FurX is a tetrameric Zn-dependent alcohol dehydrogenase (ADH) from Cupriavidus necator JMP134. The enzyme rapidly reduces furfural with NADH as the reducing power. For the first time among characterized ADHs, the high-resolution structures of all reaction steps were obtained in a time-resolved manner, thereby illustrating the complete catalytic events of NADH-dependent reduction of furfural and the dynamic Zn2+ coordination among Glu66, water, substrate and product. In the fully closed conformation of the NADH complex, the catalytic turnover proved faster than observed for the partially closed conformation due to an effective proton transfer network. The domain motion triggered by NAD(H) association/dissociation appeared to facilitate dynamic interchanges in Zn2+ coordination with substrate and product molecules, ultimately increasing the enzymatic turnover rate. NAD+ dissociation appeared to be a slow process, involving multiple steps in concert with a domain opening and reconfiguration of Glu66. This agrees with the report that the cofactor is not dissociated from FurX during ethanol-dependent reduction of furfural, in which ethanol reduces NAD+ to NADH that is subsequently used for furfural reduction. |
| Databáze: | OpenAIRE |
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