Der Einsatz eines E-Portfolios in der Lehrerfortbildung. Konzeptionelle Weiterentwicklung als Schlüssel zum erfolgreichen Einsatz

E-Portfolios, die digitale Form von Portfolios, bieten einen neuen Ansatz, um das Konzept des klassischen Portfolios wieder aufleben zu lassen. Durch das Einbinden unterschiedlicher Dateiformate wie Bild-, Audio-, Video-, PDF- und Office-Dateien, werden digitale Sammelmappen zu einer persönlichen Website-ähnlichen Struktur aufgebaut. Die Inhalte können beliebig ausgetauscht, ergänzt oder umgeordnet und dem Anlass entsprechend präsentiert werden. Dies dient dem Nutzer zur Reflexion bestimmter Sachverhalte und ermöglicht eine strukturierte Auseinandersetzung mit ausgewählten Themen. Vor diesem Hintergrund wurde ein E-Portfolio-System im Rahmen einer wissenschaftlichen Weiterbildung für Lehrerinnen und Lehrer in Baden-Württemberg eingesetzt. Die dargelegten Erfahrungen können als Grundlage für die Entwicklung einer Didaktik der wissenschaftlichen Weiterbildung herangezogen werden, welche insbesondere die Reflexion als auch die Dokumentation des Lernprozesses verankert. (DIPF/Orig.

Vanillyl alcohol oxidase from Diplodia corticola:Residues Ala420 and Glu466 allow for efficient catalysis of syringyl derivatives

Vanillyl alcohol oxidases belong to the 4-phenol oxidases family and are found predominantly in lignin-degrading ascomycetes. Systematical investigation of the enzyme family at the sequence level resulted in discovery and characterization of the second recombinantly produced VAO member, DcVAO, from Diplodia corticola. Remarkably high activities for 2,6-substituted substrates like 4-allyl-2,6-dimethoxy-phenol (3.5 ± 0.02 U mg -1) or 4-(hydroxymethyl)-2,6-dimethoxyphenol (6.3 ± 0.5 U mg -1) were observed which could be attributed to a Phe to Ala exchange in the catalytic center. In order to rationalize this rare substrate preference among VAOs, we resurrected and characterized three ancestral enzymes and performed mutagenesis analyses. The results indicate that a Cys/Glu exchange was required to retain activity for ɣ-hydroxylations and shifted the acceptance towards benzyl ethers (up to 4.0 ± 0.1 U mg -1). Our findings contribute to the understanding of the functionality of VAO enzyme group, and with DcVAO, we add a new enzyme to the repertoire of ether cleaving biocatalysts. </p

Agonistic Interventions into Public Commemorative Art:An Innovative Form of Counter-memorial Practice?

In light of recent controversies around the removal or modification of public commemorative art, such as memorials and monuments, this paper interrogates the value of competing approaches to counter-memorial practice using the framework of agonistic memory. It argues that much counter-memorial practice today, as it relates to historical memory, is dominated by a “cosmopolitan” mode that fails to offer a convincing response to the rise of right-wing populism and its instrumentalization of conflicts over public commemorative art. The article investigates two case studies of counter-memorial interventions that focus on the memory of fascism in Europe today and seeks to identify and assess emergent agonistic practices

STUDIES IN THE SYNTHESIS OF DITERPENOID ACIDS BY AN ABC APPROACH

Abstract not availabl

Structural and Mechanistical Studies on Substrate and Stereo Selectivity of the Indole Monooxygenase VpIndA1 New Avenues for Biocatalytic Epoxidations and Sulfoxidations

Crystal structure analysis of a group E flavoprotein monooxygenase in complex with substrates and products reveals a confined hydrophobic binding pocket that controls the stereoselectivity of sulfoxidation or epoxidation reactions. Molecular mechanics force field calculations and kinetic studies allowed structure based redesign of this cavity, resulting in variants with greatly enhanced stereoselectivity or acceptance of novel substrate

Flavoprotein monooxygenases: Versatile biocatalysts

Flavoprotein monooxygenases (FPMOs) are single- or two-component enzymes that catalyze a diverse set of chemo-, regio- and enantioselective oxyfunctionalization reactions. In this review, we describe how FPMOs have evolved from model enzymes in mechanistic flavoprotein research to biotechnologically relevant catalysts that can be applied for the sustainable production of valuable chemicals. After a historical account of the development of the FPMO field, we explain the FPMO classification system, which is primarily based on protein structural properties and electron donor specificities. We then summarize the most appealing reactions catalyzed by each group with a focus on the different types of oxygenation chemistries. Wherever relevant, we report engineering strategies that have been used to improve the robustness and applicability of FPMOs.BT/Biocatalysi