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Flavin Coenzymes

  1. Sandro Ghisla1,
  2. Dale E Edmondson2

Published Online: 15 SEP 2009

DOI: 10.1002/9780470015902.a0000654.pub2

eLS

eLS

How to Cite

Ghisla, S. and Edmondson, D. E. 2009. Flavin Coenzymes. eLS. .

Author Information

  1. 1

    University of Konstanz, Konstanz, Germany

  2. 2

    Emory University, Atlanta, Georgia, USA

Publication History

  1. Published Online: 15 SEP 2009

This is not the most recent version of the article. View current version (15 SEP 2014)

Abstract

Flavins are yellow chromophores in organisms from bacteria to humans and essential for practically all metabolic processes. They occur in nature in a variety of forms. The core of the flavin cofactor is the (iso)alloxazine nucleus with the most common forms as FMN (flavin mononucleotide) and FAD (flavin-adenine dinucleotide). A number of flavin cofactors are covalently linked to their apoproteins. The covalent linkage is, in general, via a modification of the benzene subnucleus and functional groups of amino acid side chains. As cofactors, flavins are distinguished by their ability to catalyse a variety of different processes involving oxidation-reduction (redox) reactions.

Key Concepts

  • Chemical variation of a basic molecule (the isoalloxazine) leads to several (modified) coenzymes that differ significantly in their catalytic properties.

  • The type and position of the modification is a key determinant for the properties of the (modified) coenzyme.

  • The cofactor interacts with the protein in many different ways. These, in turn, affect the properties of the cofactor as a catalyst. The result is a disparate selection of catalytic functions.

Keywords:

  • FMN;
  • FAD;
  • flavoprotein;
  • alloxazine;
  • cofactor;
  • redox