Regulation of Redox Potential of a Pterin Derivative Bound to a Ruthenium(II) Complex by Intermolecular Hydrogen Bonding with Nucleobases†
This work was supported by Grants‐in‐Aid (Nos. 23750014, 20108010, 21350035, and 20108001), a Global COE program, “The Global Education and Research Center for Bio‐Environmental Chemistry” from the Japan Society of Promotion of Science (JSPS), the Ministry of Education, Science, and Technology of Japan, and by KOSEF/MEST through WCU project (R31‐2008‐000‐10010‐0) of Korea.
Abstract
Potential control: A RuII‐bound pterin forms a stable hydrogen‐bonding adduct with a guanine derivative through three‐point recognition. A large positive shift of the reduction potential of the pterin ligand up to +320 mV is observed (see picture). For the thymine derivative, the mode of hydrogen bonding is altered. Regulation of redox potentials of a pterin coenzyme by noncovalent interaction is demonstrated.





