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PubMed · 10600716

Model systems for redox cofactor activity.

Abstract

Numerous model studies of organic redox cofactor activity have appeared in the latter half of 1998 and the first half of 1999. These investigations include the use of solution models to explore flavin-dependent, quinone-dependent and pyrroloquinone-dependent redox processes, the exploration of flavin and quinone redox events using organized interfaces, and the application of computational methods to increase the understanding of flavin-catalyzed, nicotinamide-catalyzed and quinone-catalyzed redox processes.

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BibTeXRIS

V M Rotello. 1999. Model systems for redox cofactor activity.. https://doi.org/10.1016/s1367-5931(99)00035-6

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An N1-hydrogen bonding model for flavin coenzyme.

A model flavin possessing a specific hydrogen bond to the N1-position has been synthesized. The redox potential has been measured in aqueous buffer and found to be shifted +21 mV as compared to a similar flavin lacking this hydrogen bond. The reaction of the N1-hydrogen-bonding model with sulfite and 1-benzyl-dihydronicotinamide were examined and compared with the non-hydrogen-bonded flavin. The N1-hydrogen bond did not accelerate the rate of sulfite ion or hydride addition to N5, however the N5-sulfite complex was stabilized by nearly 4-fold over a non-hydrogen-bonding model. The model flavins were also studied computationally.

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