Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1927217 | Archives of Biochemistry and Biophysics | 2007 | 6 Pages |
Abstract
Alcohol oxidase (AO) is a peroxisomal, homo-octameric flavoenzyme, which catalyzes methanol oxidation in methylotrophic yeast. Here, we report on the generation of soluble, FAD-lacking AO monomers. Using steady-state fluorescence, fluorescence correlation spectroscopy, circular dichroism and static light scattering approaches, we demonstrate that FAD-lacking AO monomers are formed upon incubation of purified, native octameric AO in a solution containing 50% dimethylsulfoxide (DMSO). Upon removal of DMSO the protein remained monomeric and soluble and did not contain FAD. Binding experiments revealed that the AO monomers bind to purified pyruvate carboxylase, a protein that plays a role in the formation of enzymatically active AO octamers in vivo.
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Authors
Nina V. Visser, Dongyuan Wang, Will A. Stanley, Matthew R. Groves, Matthias Wilmanns, Marten Veenhuis, Ida J. van der Klei,