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Träfflista för sökning "WFRF:(Lisdat Fred) srt2:(2012)"

Sökning: WFRF:(Lisdat Fred) > (2012)

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1.
  • Feifel, Sven C., et al. (författare)
  • Catalytically Active Silica Nanoparticle-Based Supramolecular Architectures of Two Proteins - Cellobiose Dehydrogenase and Cytochrome c on Electrodes
  • 2012
  • Ingår i: Langmuir. - : American Chemical Society (ACS). - 0743-7463 .- 1520-5827. ; 28:25, s. 9189-9194
  • Tidskriftsartikel (refereegranskat)abstract
    • Artificial nanobiomolecular architectures that follow natural examples in protein assembly become more and more important from basic and applied points of view. Our study describes the investigation on cellobiose dehydrogenase (CDH), cytochrome c (cyt c), and silica nanoparticles (SiNP's) for the construction of fully catalytically active supramolecular architectures on electrodes. We report on intraprotein, interprotein, and direct electron-transfer reaction cascades of cellobiose dehydrogenase and cytochrome c immobilized in multiple supramolecular layers. Carboxy-modified SiNP's are used to provide an artificial matrix, which enables protein arrangement in an electroactive form. Direct and interprotein electron transfer has been established for a two-protein system with CDH and cyt c in a layered architecture for the first time. We also highlight that the glycosylation of CDH and the silica nanoparticle size play key roles in the mode of operation in such a complex system. The response of the specific substrate, here lactose, can be tuned by the number of immobilized nanobiomolecular layers.
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2.
  • Sarauli, David, et al. (författare)
  • Investigation of the mediated electron transfer mechanism of cellobiose dehydrogenase at cytochrome c-modified gold electrodes
  • 2012
  • Ingår i: Bioelectrochemistry. - : Elsevier BV. - 1878-562X .- 1567-5394. ; 87, s. 9-14
  • Tidskriftsartikel (refereegranskat)abstract
    • The present study reports on the comparison of direct and mediated electron transfer pathways in the interaction of the fungal enzyme cellobiose dehydrogenase (CDH) with the redox protein cytochrome c (cyt c) immobilised at a modified gold electrode surface. Two types of CDHs were chosen for this investigation: a basidiomycete (white rot) CDH from Trametes villosa and a recently discovered ascomycete from the thermophilic fungus Corynascus thermophilus. The choice was based on the pH-dependent interaction of these enzymes with cyt c in solution containing the substrate cellobiose (CB). Both enzymes show rather similar catalytic behaviour at lower pH, dominated by a direct electron exchange with the electrode. With increasing pH, however, also cyt c-mediated electron transfer becomes possible. The pH-dependent behaviour in the presence and in the absence of cyt c is analysed and the potential reaction mechanism for the two enzymes with a different pH-behaviour is discussed. (c) 2011 Published by Elsevier B.V.
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  • Resultat 1-2 av 2
Typ av publikation
tidskriftsartikel (2)
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refereegranskat (2)
Författare/redaktör
Gorton, Lo (2)
Ludwig, Roland (2)
Lisdat, Fred (2)
Haltrich, Dietmar (1)
Feifel, Sven C. (1)
Sarauli, David (1)
Lärosäte
Lunds universitet (2)
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Engelska (2)
Forskningsämne (UKÄ/SCB)
Naturvetenskap (2)
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2012 (2)Ta bort avgränsningen

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