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Results 1 - 4 of 4
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construction of a plasmid containing genes of apo-allophycocyanin alpha-subunit without chromophore and chromophore synthetases HO1, i.e. ferredoxin-dependent heme oxygenase, and PcyA, i.e. phycocyanobilin:ferredoxin oxidoreductase, and expression in Escherichia coli. Holo-allophycocyanin, i.e. allophycocyanin alpha-subunit with chromophore, can be synthesized by autocatalysis in Escherichia coli. Recombinant holo-allophycocyanin alpha-subunit shows the same spectral and fluorescent properties as phycocyanin and serves as a good substitute for native phycocyanin for fluorescent tagging. Recombinant allophycocyanin alpha-subunit can inhibit hydroxyl and peroxyl radicals more strongly than holo-allophycocyanin alpha-subunit and native allophycocyanin
co-expression of heme oxygenase in a single operon in conjunction with apophytochrome, is a system to produce phytochromes with various chromophores in Escherichia coli, metabolic engineering of bacteria for the production of various bilins for assembly into phytochromes will facilitate the molecular analysis of photoreceptors
conserved histidine and aspartate residues essential for the catalytic activity of the enzyme, direct role of the His85-Asp102 pair in exovinyl reduction of biliverdin IXa
phycocyanobilin-CpcB(C155I) and phycocyanobilin-PecB(C155I) are also biosynthesized heterologously in vivo, when cpeS is introduced into Escherichia coli with cpcB(C155I) or pecB(C155I), respectively, together with genes ho1 and pcyA
Results 1 - 4 of 4