64183-66-0Relevant academic research and scientific papers
Conversion of a Dehalogenase into a Nitroreductase by Swapping its Flavin Cofactor with a 5-Deazaflavin Analogue
Su, Qi,Boucher, Petrina A.,Rokita, Steven E.
, p. 10862 - 10866 (2017/08/30)
Natural and engineered nitroreductases have rarely supported full reduction of nitroaromatics to their amine products, and more typically, transformations are limited to formation of the hydroxylamine intermediates. Efficient use of these enzymes also requires a regenerating system for NAD(P)H to avoid the costs associated with this natural reductant. Iodotyrosine deiodinase is a member of the same structural superfamily as many nitroreductases but does not directly consume reducing equivalents from NAD(P)H, nor demonstrate nitroreductase activity. However, exchange of its flavin cofactor with a 5-deazaflavin analogue dramatically suppresses its native deiodinase activity and leads to significant nitroreductase activity that supports full reduction to an amine product in the presence of the convenient and inexpensive NaBH4.
Rational improvement of the synthesis of 1-deazariboflavin
Wood, Andrew C.,Knight, David W.,Richter, Gerald
, p. 1679 - 1683 (2015/03/18)
The cofactor forms of riboflavin (FMN and FAD) play a crucial role in the mediation of both enzymatic processes and light perception by photo-sensitive proteins, and thus structural analogues of this chromophore are highly useful tools to assist in the elucidation of enzymatic mechanisms. 1-Deazariboflavin has been rarely utilised for this purpose, due in part to its previously difficult and inefficient synthesis. Recent examination has enabled a remarkable improvement in the overall synthetic yield from 11.0 to 61.3%, allowing reliable production of 1-deazariboflavin for use as a tool in enzymatic mechanistic determination.
Synthesis and electrochemical properties of structurally modified flavin compounds
Mansurova, Madina,Koay, Melissa S.,Gaertner, Wolfgang
supporting information; experimental part, p. 5401 - 5406 (2009/05/07)
Four structurally modified flavin compounds have been synthesized and characterized for their redox potential by chemical reduction with sodium dithionite. Besides the previously reported 1- and 5-deazariboflavin, a 7,8-didemethyl derivative and an 8-isopropylriboflavin have been obtained. The synthesis of these compounds started in all cases from appropriately substituted anilines that were condensed with the ribityl chain, followed by completion of the annealed three-ring structure. The didemethyl- and the isopropyl compounds gave absorption maxima similar to riboflavin (436 and 448 nm, respectively), whereas 1-deazariboflavin showed a bathochromically shifted absorption (λmax = 537 nm), and that of 5-deazariboflavin was hypsochromically shifted (λmax = 400 nm). The midpoint potentials (E0′) of the four modified flavin compounds were determined by potentiometric titration, using riboflavin as a reference compound. Both alkyl-modified flavins showed slightly less negative midpoint potentials, whereas both deaza compounds had more negative midpoint values compared to the reference compound. Wiley-VCH Verlag GmbH & Co. KGaA, 2008.
Improved Chemical Syntheses of 1- and 5-Deazariboflavin
Carlson, Erin E.,Kiessling, Laura L.
, p. 2614 - 2617 (2007/10/03)
The cofactor flavin adenine dinucleotide (FAD) is required for the catalytic activity of a large class of enzymes known as flavoenzymes. Because flavin cofactors participate in catalysis via a number of different mechanisms, isoalloxazine analogues are valuable for mechanistic studies. We report improved chemical syntheses for the preparation of the two key analogues, 5-deazariboflavin and 1-deazariboflavin.
