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- Hockenjos, Vreni, 1972-
(author)
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Picturing Dissolving Views : August Strindberg and the Visual Media of His Age
- 2007
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Doctoral thesis (other academic/artistic)abstract
- The subject of this study is August Strindberg’s interaction with the visual media of his day. Its dual aim is to examine Strindberg’s work in the light of media history and to allow Strindberg’s work in turn to illuminate the media history of the fin de siècle. Taking its cue from the commonplace scholarly observation that Strindberg’s drama, particularly that of his later phase, is strikingly “cinematic”, it asks: What do such comparisons really tell us about Strindberg’s art and what, if anything, do they tell us about cinema?The thesis of this study is that the putatively “cinematic” style of Strindberg’s writings can only be understood against the backdrop of a mass culture, oriented towards the visual sense, which was undergoing rapid expansion at the turn of the last century. In devising his “dream play techniques”, it argues, Strindberg both drew on and reacted against various image-based modes of representation that had become extremely widespread in the late nineteenth century. The loss of reality that is so prominent a feature of works such as To Damascus (1898) or A Dream Play (1901) should in this sense be regarded as marked by an experience of mediatization, that is, the steady incorporation of all aspects of daily life by mass media technologies. Shifting the spotlight away from cinema, a critical encounter with Strindberg’s work can cast light on largely overlooked media practices such as magic lantern or Sciopticon exhibition, panoramic entertainments, instantaneous photography, and the introduction of the halftone process in printing. At the same time as it unsettles received notions of Strindberg’s drama as “cinematic”, the study seeks to show how the writings of this revolutionary artist can provide fresh material for a reassessment of life in a media-saturated age.
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| 2. |
- Kolberg, Matthias, et al.
(author)
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A new tyrosyl radical on Phe208 as ligand to the diiron center in Escherichia coli ribonucleotide reductase, mutant R2-Y122H. Combined x-ray diffraction and EPR/ENDOR studies.
- 2005
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In: J Biol Chem. - 0021-9258. ; 280:12, s. 11233-11246
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Journal article (other academic/artistic)abstract
- The R2 protein subunit of class I ribonucleotide reductase (RNR) belongs to a structurally related family of oxygen bridged diiron proteins. In wild-type R2 of Escherichia coli, reductive cleavage of molecular oxygen by the diferrous iron center generates a radical on a nearby tyrosine residue (Tyr122), which is essential for the enzymatic activity of RNR, converting ribonucleotides into deoxyribonucleotides. In this work, we characterize the mutant E. coli protein R2-Y122H, where the radical site is substituted with a histidine residue. The x-ray structure verifies the mutation. R2-Y122H contains a novel stable paramagnetic center which we name H, and which we have previously proposed to be a diferric iron center with a strongly coupled radical, Fe(III)Fe(III)R.. Here we report a detailed characterization of center H, using 1H/2H -14N/15N- and 57Fe-ENDOR in comparison with the Fe(III)Fe(IV) intermediate X observed in the iron reconstitution reaction of R2. Specific deuterium labeling of phenylalanine residues reveals that the radical results from a phenylalanine. As Phe208 is the only phenylalanine in the ligand sphere of the iron site, and generation of a phenyl radical requires a very high oxidation potential, we propose that in Y122H residue Phe208 is hydroxylated, as observed earlier in another mutant (R2-Y122F/E238A), and further oxidized to a phenoxyl radical, which is coordinated to Fe1. This work demonstrates that small structural changes can redirect the reactivity of the diiron site, leading to oxygenation of a hydrocarbon, as observed in the structurally similar methane monoxygenase, and beyond, to formation of a stable iron-coordinated radical.
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