Publications by authors named "Ulrich Scholten"

Remote teaching in the tertiary education sector is a relatively common practice, and the implementation of digital solutions in chemistry teaching offers many new opportunities and tools. A survey was conducted after 3 months of emergency remote teaching linked to the COVID-19 pandemic and showed that half of the students estimated it was difficult to study remotely, and reported they had to invest more time compared to classroom teaching, which led to a drop in motivation. Professors also noted that the time necessary to invest in order to produce digital teaching content was enormous.

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The reduction rates of horse heart ferricytochrome c by amalgamated zinc or by electrolysis at fixed potential on a mercury pool as the cathode have been measured in a buffered solution at pH 7.5 by absorption spectrophotometry. In both cases, the reaction was strongly accelerated by the presence of the optically active complexes Lambda-[Cr(III)((S,S)-promp)H(2)O](+) (H(2)promp = N,N'-[(pyridine-2,6-diyl)bis(methylene)]-bis[(S)-proline]), Delta-[Cr(III)((R,R)-alamp)H(2)O](+) (H(2)alamp = N,N'-[(pyridine-2,6-diyl)bis(methylene)]-bis[(R)-alanine]) and Lambda-[Cr(III)((S,S)-alamp)(H(2)O)(2)](+).

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The protonation of a sterically crowded [N2S6] macropentacycle (1) with 1 equiv of CF3SO3H in CDCl3 is slow and gives the singly (oo(+) [1 x H](+)) and doubly (o(+)o(+) [1 x 2H](2+)) protonated forms as kinetic products, the i(+)o form of [1 x H](+) being the thermodynamic product. i(+)o [1 x H](+) is C3 helically chiral in the solid state and in solution. The barrier to racemization (DeltaG(double dagger)) of the [1 x H](+) propeller is >71 kJ mol(-1).

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Optically active cobalt(II) complexes are used as reducing agents in the electron-transfer reaction involving horse heart cytochrome c. Analysis of the circular dichroism (CD) spectra of reaction products indicates that the corresponding cobalt(III) species of both enantiomers of [CoII(alamp)] (H2alamp=N,N'-[(pyridine-2,6-diyl)bis(methylene)]-bis[alanine]) are partly attached to the protein during electron transfer by coordination to an imidazole unit of one of the histidine residues. His-26 and His-33 are both solvent exposed, and the results suggest that one of these histidine residues acts as a bridge in the electron transfer to and from the haem iron of cytochrome c.

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