2018年
The Rich Chemistry of Weak Interaction in a Blue Copper Protein, Pseudoazurin
International Conference of Coordination Chemistry, 2018
- ,
- 記述言語
- 英語
- 会議種別
- 口頭発表（招待・特別）
- 開催地
- Sendai
Noncovalent weak interactions play important roles in biological systems1. In particular, such interactions in the second-coordination shell of metal ions in proteins modulate the structure and reactivity of the metal ion site in functionally significant ways.
Recently, we have demonstrated the perturbation of weak non-covalent interaction on the structure and properties of copper site in a blue copper protein, pseudoazurin (PAz)2. PAz is well known to work as an electron transfer protein to NO2- reductase and N2O reductase in denitrifying bacteria3. The weak interaction at Met16 with a copper coordinated histidine (His81) imidazole ring in the second coordination sphere provides not only for the modulation of PAz properties but also the protein stability4. We also would like to report the recent solution structure analysis by small angle neutron scattering in this lecture.
Recently, we have demonstrated the perturbation of weak non-covalent interaction on the structure and properties of copper site in a blue copper protein, pseudoazurin (PAz)2. PAz is well known to work as an electron transfer protein to NO2- reductase and N2O reductase in denitrifying bacteria3. The weak interaction at Met16 with a copper coordinated histidine (His81) imidazole ring in the second coordination sphere provides not only for the modulation of PAz properties but also the protein stability4. We also would like to report the recent solution structure analysis by small angle neutron scattering in this lecture.