Novel cofactor derivatives and cofactor-based models

https://doi.org/10.1016/S1367-5931(98)80114-2Get rights and content

Abstract

In 1997 and the first half of 1998, numerous publications appeared reporting studies of cofactors and their analogues in classical model systems and in enzyme-catalyzed reactions directed at understanding the enzymatic reactions of their natural cofactors. Model systems based on flavins have provided new insights into enzymatic modulation of the flavin reduction potential, and enzymatic reactions of coenzyme A analogues and derivatives have been employed in several studies of coenzyme A utilizing enzymes. Coenzyme B12 analogues have been utilized as alternate cofactors for B12-utilizing enzymes, while pyrroloquinoline quinone esters and analogues have been employed in model studies of the reactions of quinoprotein-catalyzed reactions.

References (31)

  • A Niemz et al.

    Model systems for flavoenzyme activity: one- and two-electron reduction of flavins in aprotic hydrophobic environments (of special interest)

    J Am Chem Soc

    (1997)
  • EC Breinlinger et al.

    Model systems for flavoenzyme activity. Stabilization of the Flavin Radical anion through specific hydrogen bond interactions

    J Am Chem Soc

    (1995)
  • R Deans et al.

    Electrochemical control of recognition processes. A three-component molecular switch

    J Am Chem Soc

    (1997)
  • MD Greaves et al.

    Model systems for flavoenzyme activity. Specific hydrogen bond recognition of flavin in a silicate sol-gel

    J Am Chem Soc

    (1997)
  • R Blonder et al.

    Application of a nitrospiropyran-FAD-reconstituted glucose oxidase and charged electron mediators as optobioelectronic assemblies for the amperometric transduction of recorded optical signals: control of the ‘on’-‘off’ direction of the photoswitch

    J Am Chem Soc

    (1997)
  • Cited by (0)

    View full text