An artificial redox coenzyme based on a triazine dye template
A series of nicotinamide-containing compounds based on the structure of a triazine dye, C.I. Reactive Blue 2, which is known to interact at the coenzyme-binding sites of several NAD(P)(H)-dependent dehydrogenases, 1,2 were designed, synthesized, and characterized. The preparation of these compounds...
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Published in | Enzyme and microbial technology Vol. 18; no. 8; pp. 570 - 580 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
Amsterdam
Elsevier Inc
1996
Elsevier Science |
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Abstract | A series of nicotinamide-containing compounds based on the structure of a triazine dye, C.I. Reactive Blue 2, which is known to interact at the coenzyme-binding sites of several NAD(P)(H)-dependent dehydrogenases,
1,2
were designed, synthesized, and characterized. The preparation of these compounds is described. Reduction of the coenzyme mimics with sodium borohydride led to an increase in absorption at 356 nm, analogous to the behavior of the natural coenzyme, NAD
+.
3 When incubated with horse liver alcohol dehydrogenase and ethanol at 25°C and pH 9.0, one of the mimics, Blue N-3, was converted into a new compound with an increased absorption at 356 nm and an
R
f
value on thin-layer chromatography identical to that of the reduced form produced by treatment with sodium borohydride. The oxidized and reduced forms of Blue N-3 could be separated by reverse-phase ion pair high-performance liquid chromatography. This technique could be used to measure the extent of Blue N-3 reduction: Approximately 90 turnovers were calculated for each enzyme active site over a 48-h period. Gas chromatography analysis suggested that ethanol was simultaneously converted to acetaldehyde. Blue N-3 represents the first example of a new generation of potentially inexpensive, stable, and active biomimetic redox coenzymes. |
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AbstractList | A series of nicotinamide-containing compounds based on the structure of a triazine dye, C.I. Reactive Blue 2, which is known to interact at the coenzyme-binding sites of several NAD(P)(H)-dependent dehydrogenases,
1,2
were designed, synthesized, and characterized. The preparation of these compounds is described. Reduction of the coenzyme mimics with sodium borohydride led to an increase in absorption at 356 nm, analogous to the behavior of the natural coenzyme, NAD
+.
3 When incubated with horse liver alcohol dehydrogenase and ethanol at 25°C and pH 9.0, one of the mimics, Blue N-3, was converted into a new compound with an increased absorption at 356 nm and an
R
f
value on thin-layer chromatography identical to that of the reduced form produced by treatment with sodium borohydride. The oxidized and reduced forms of Blue N-3 could be separated by reverse-phase ion pair high-performance liquid chromatography. This technique could be used to measure the extent of Blue N-3 reduction: Approximately 90 turnovers were calculated for each enzyme active site over a 48-h period. Gas chromatography analysis suggested that ethanol was simultaneously converted to acetaldehyde. Blue N-3 represents the first example of a new generation of potentially inexpensive, stable, and active biomimetic redox coenzymes. A series of nicotinamide-containing compounds based on the structure of a triazine dye, C.I. Reactive Blue 2, which is known to interact at the coenzyme-binding sites of several NAD(P)(H)-dependent dehydrogenases, were designed, synthesized, and characterized. The preparation of these compounds is described. Reduction of the coenzyme mimics with sodium borohydride led to an increase in absorption at 356 nm, analogous to the behavior of the natural coenzyme, NAD super(+). When incubated with horse liver alcohol dehydrogenase and ethanol at 25 degree C and pH 9.0, one of the mimics, Blue N-3, was converted into a new compound with an increased absorption at 356 nm and an R sub(f) value on thin-layer chromatography identical to that of the reduced form produced by treatment with sodium borohydride. The oxidized and reduced forms of Blue N-3 could be separated by reverse-phase ion pair high-performance liquid chromatography. This technique could be used to measure the extent of Blue N-3 reduction: Approximately 90 turnovers were calculated for each enzyme active site over a 48-h period. Gas chromatography analysis suggested that ethanol was simultaneously converted to acetaldehyde. Blue N-3 represents the first example of a new generation of potentially inexpensive, stable, and active biomimetic redox coenzymes. |
Author | Vivian Stead, C. Ansell, Richard J. Lowe, Christopher R. Burton, Steven J. |
Author_xml | – sequence: 1 givenname: Steven J. surname: Burton fullname: Burton, Steven J. – sequence: 2 givenname: C. surname: Vivian Stead fullname: Vivian Stead, C. – sequence: 3 givenname: Richard J. surname: Ansell fullname: Ansell, Richard J. – sequence: 4 givenname: Christopher R. surname: Lowe fullname: Lowe, Christopher R. |
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Keywords | triazine dyes Biomimetic coenzyme horse liver alcohol dehydrogenase coenzyme analog Dyes Purification Enzyme Liver Alcohol dehydrogenase Coenzyme Vertebrata Mammalia Analog Horse Triazine derivatives Nicotinamide Oxidoreductases Perissodactyla Chemical synthesis Ungulata Physicochemical properties Enzymatic reaction |
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Snippet | A series of nicotinamide-containing compounds based on the structure of a triazine dye, C.I. Reactive Blue 2, which is known to interact at the... |
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SubjectTerms | Biological and medical sciences Biomimetic coenzyme Biotechnology coenzyme analog Enzyme engineering Fundamental and applied biological sciences. Psychology horse liver alcohol dehydrogenase Methods. Procedures. Technologies Miscellaneous triazine dyes |
Title | An artificial redox coenzyme based on a triazine dye template |
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