JBIC Journal of Biological Inorganic Chemistry

, Volume 13, Issue 3, pp 321–333

Control of redox reactivity of flavin and pterin coenzymes by metal ion coordination and hydrogen bonding

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DOI: 10.1007/s00775-008-0343-1

Cite this article as:
Fukuzumi, S. & Kojima, T. J Biol Inorg Chem (2008) 13: 321. doi:10.1007/s00775-008-0343-1

Abstract

The electron-transfer activities of flavin and pterin coenzymes can be fine-tuned by coordination of metal ions, protonation and hydrogen bonding. Formation of hydrogen bonds with a hydrogen-bond receptor in metal–flavin complexes is made possible depending on the type of coordination bond that can leave the hydrogen-bonding sites. The electron-transfer catalytic functions of flavin and pterin coenzymes are described by showing a number of examples of both thermal and photochemical redox reactions, which proceed by controlling the electron-transfer reactivity of coenzymes with metal ion binding, protonation and hydrogen bonding.

Keywords

CofactorElectron transferPhotoreductionFlavinPterin

Copyright information

© SBIC 2008

Authors and Affiliations

  1. 1.Department of Material and Life Science, Graduate School of EngineeringOsaka University, SORST, Japan Science and Technology AgencySuita, OsakaJapan