85923-80-4Relevant academic research and scientific papers
Alteration of the substrate specificity of the angular dioxygenase carbazole 1,9a-dioxygenase
Uchimura, Hiromasa,Horisaki, Tadafumi,Umeda, Takashi,Noguchi, Haruko,Usami, Yusuke,Li, Li,Terada, Tohru,Nakamura, Shugo,Shimizu, Kentaro,Takemura, Tetsuo,Habe, Hiroshi,Furihata, Kazuo,Omori, Toshio,Yamane, Hisakazu,Nojiri, Hideaki
body text, p. 3237 - 3248 (2009/04/10)
Carbazole 1,9a-dioxygenase (CARDO) consists of terminal oxygenase (CARDO-O) and electron transport components. CARDO can catalyze specific oxygenation for various substrates: angular dioxygenation for carbazole and dibenzo-p-dioxin, lateral dioxygenation for anthracene, and monooxygenation for methylene carbon of fluorene and sulfide sulfur of dibenzothiophene. To elucidate the molecular mechanism determining its unique substrate specificity, 17 CARDO-O site-directed mutants at amino acid residues I262, F275, Q282, and F329, which form the substrate-interacting wall around the iron active site by CARDO-O crystal structure, were generated and characterized. F329 replacement dramatically reduced oxygenation activity. However, several mutants produced different products from the wild-type enzyme to a large extent: I262V and Q282Y (1-hydroxycarbazole), F275W (4-hydroxyfluorene), F275A (unidentified cis-dihydrodiol of fluoranthene), and I262A and I262W (monohydroxydibenzothiophenes). These results suggest the possibility that the respective substrates bind to the active sites of CARDO-O mutants in a different orientation from that of the wild-type enzyme.
Synthesis of the Isomeric Phenols and the trans-2,3-Dihydrodiol of Fluoranthene
Rice, Joseph E.,LaVoie, Edmond J.,Hoffmann, Dietrich
, p. 2360 - 2363 (2007/10/02)
The syntheses of 1-hydroxy-, 2-hydroxy-, 7-hydroxy-, and 8-hydroxyfluoranthene, as well as that of trans-2,3-dihydroxy-2,3-dihydrofluoranthene, are described.UV and fluorescence spectra are reported for all five isomeric fluoranthenols as well as for the
