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.
| Original language | English |
|---|---|
| Pages (from-to) | 321-333 |
| Number of pages | 13 |
| Journal | Journal of Biological Inorganic Chemistry |
| Volume | 13 |
| Issue number | 3 |
| DOIs | |
| State | Published - Mar 2008 |
Bibliographical note
Funding Information:Acknowledgments The authors gratefully acknowledge the contributions of their collaborators and coworkers mentioned in the references. The authors acknowledge continuous support of their study by Grants-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology, Japan.
Keywords
- Cofactor
- Electron transfer
- Flavin
- Photoreduction
- Pterin