Control of redox reactivity of flavin and pterin coenzymes by metal ion coordination and hydrogen bonding.
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.
Fukuzumi
Shunichi
S
Department of Material and Life Science, Graduate School of Engineering, Osaka University, SORST, Japan Science and Technology Agency, 2-1 Yamada-oka, Suita, Osaka, 565-0871, Japan. fukuzumi@chem.eng.osaka-u.ac.jp
Kojima
Takahiko
T
D003067:Coenzymes / Q000737:chemistry*; D004583:Electrons; D005415:Flavins / Q000737:chemistry*; D006860:Hydrogen Bonding; D008670:Metals / Q000737:chemistry*; D008958:Models, Molecular; D010084:Oxidation-Reduction; D011622:Pterins / Q000737:chemistry*
D003067:Coenzymes; D005415:Flavins; D008670:Metals; D011622:Pterins