ArticleProtein science : a publication of the Protein Society2008
Relevance of the flavin binding to the stability and folding of engineered cholesterol oxidase containing noncovalently bound FAD.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 33 citations in OpenAlex.
- High-efficiency secretion expression of FAD-dependent glucose dehydrogenase in Pichia pastoris via signal peptide optimization and redox cofactor enhancement.Bioprocess and biosystems engineering · 2026Article
- Mechanistic insights into redox activity and catalytic determinants of the haloarchaeal flavin-dependent oxidoreductasebioRxiv : the preprint server for biology · 2026Article
- Stabilization of the catalytically active structure of a molybdenum-dependent formate dehydrogenase depends on a highly conserved lysine residue.The FEBS journal · 2025Article
- Flavin transferase ApbE: From discovery to applications.The Journal of biological chemistry · 2025Review
- Fixing Flavins: Hijacking a Flavin Transferase for Equipping Flavoproteins with a Covalent Flavin Cofactor.Journal of the American Chemical Society · 2023Article
- Thermodynamic Evaluation of the Interactions between Anticancer Pt(II) Complexes and Model Proteins.Molecules (Basel, Switzerland) · 2021Article
- Why the Flavin Adenine Dinucleotide (FAD) Cofactor Needs To Be Covalently Linked to Complex II of the Electron-Transport Chain for the Conversion of FADHChemistry (Weinheim an der Bergstrasse, Germany) · 2018Article
- Contribution of flavin covalent linkage with histidine 99 to the reaction catalyzed by choline oxidase.The Journal of biological chemistry · 2009Article
- Functional roles of the 6-S-cysteinyl, 8alpha-N1-histidyl FAD in glucooligosaccharide oxidase from Acremonium strictum.The Journal of biological chemistry · 2008Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The flavoprotein cholesterol oxidase (CO) from Brevibacterium sterolicum is a monomeric flavoenzyme containing one molecule of FAD cofactor covalently linked to His69. The elimination of the covalent link following the His69Ala substitution was demonstrated to result in a significant decrease in activity, in the midpoint redox potential of the flavin, and in stability with respect to the wild-type enzyme, but does not modify the overall structure of the enzyme. We used CO as a model system to dissect the changes due to the elimination of the covalent link between the flavin and the protein (by comparing the wild-type and H69A CO holoproteins) with those due to the elimination of the cofactor (by comparing the holo- and apoprotein forms of H69A CO). The apoprotein of H69A CO lacks the characteristic tertiary structure of the holoprotein and displays larger hydrophobic surfaces; its urea-induced unfolding does not occur by a simple two-state mechanism and is largely nonreversible. Minor alterations in the flavin binding region are evident between the native and the refolded proteins, and are likely responsible for the low refolding yield observed. A model for the equilibrium unfolding of H69A CO that also takes into consideration the effects of cofactor binding and dissociation, and thus may be of general significance in terms of the relationships between cofactor uptake and folding in flavoproteins, is presented.
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