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In Prismatik's Scarlet Portrait Parlor (2020) poetry and code uncannily appear one and the same. This results in a work that is both familiar and strange, and this, along with Scarlet Portrait Parlor 's brevity, simplicity of construction, and immediate recognizability as a work of literature (a sonnet) that is also executable source code producing a work of electronic literature, has the potential to intrigue students and textual scholars unfamiliar with and perhaps resistant to Critical Code Studies (CCS). A study of Prismatik's work also has the potential to refine some simplistic judgements in CCS scholarship about the efficacy of code that emulates natural, human language. This case study aims to elaborate the value of Scarlet Portrait Parlor as a rich example of how poetry, programming, and interactive fiction can be intertwined if not blurred in a single text and to act as a catalyst for generative discussions about the overlapping and intertwining of natural languages, programming languages, creative writing, and coding. This case study aims to elaborate the value of Scarlet Portrait Parlor as a rich example of how poetry, programming, and interactive fiction can be intertwined if not blurred in a single text. [ABSTRACT FROM AUTHOR]

Abstract: AtCCD1 and AtNCED3 are related carotenoid cleavage enzymes from Arabidopsis thaliana that catalyze the oxidative cleavage of, respectively, the 9,10 (9',10') double bonds of carotenoid substrates such as β-carotene, [...]

Pseudomonas fluorescens strain KU-7 is a prototype microorganism that metabolizes 2-nitrobenzoate (2-NBA) via the formation of 3-hydroxyanthranilate (3-HAA), a known antioxidant and reductant. The initial two steps leading to the sequential formation of 2-hydroxy/aminobenzoate and 3-HAA are catalyzed by a NADPH-dependent 2-NBA nitroreductase (NbaA) and 2-hydroxylaminobenzoate mutase (NbaB), respectively. The 216-amino-acid protein NbaA is 78% identical to a plasmid-encoded hypothetical conserved protein of Polaromonas strain JS666; structurally, it belongs to the homodimeric NADH:flavin mononucleotide (FMN) oxidoreductase-like fold family. Structural modeling of complexes with the flavin, coenzyme, and substrate suggested specific residues contributing to the NbaA catalytic activity, assuming a ping-pong reaction mechanism. Mutational analysis supports the roles of Asn40, Asp76, and Glu113, which are predicted to form the binding site for a divalent metal ion implicated in FMN binding, and a role in NADPH binding for the 10-residue insertion in the [beta]5-[alpha]2 loop. The 181-amino-acid sequence of NbaB is 35% identical to the 4-hydroxylaminobenzoate lyases (PnbBs) of various 4-nitrobenzoate-assimilating bacteria, e.g., Pseudomonas putida strain TW3. Coexpression of nbaB with nbaA in Escherichia coli produced a small amount of 3-HAA from 2-NBA, supporting the functionality of the nbaB gene. We also showed by gene knockout and chemotaxis assays that nbaY, a chemoreceptor NahY homolog located downstream of the nbaA gene, is responsible for strain KU-7 being attracted to 2-NBA. NbaY is the first chemoreceptor in nitroaromatic metabolism to be identified, and this study completes the gene elucidation of 2-NBA metabolism that is localized within a 24-kb chromosomal locus of strain KU-7. doi:10.1128/JB.01098-06