Sugiura Y
Bioinorg Chem. 1978;8(5):453-60. doi: 10.1016/s0006-3061(00)80280-x.
The electronic properties of 2:1 sulfhydryl- and imidazole-containing peptide-Co(II) complexes have been investigated and compared with those of Co(II)-substituted "blue" copper proteins. The Co(II) complexes of N-mercaptoacetyl-L-histidine and 3-mercaptopropionyl-L-histidine gave the ligand field parameters of deltat = 4110 and B = 756 cm(-1), and of deltat = 4120 and B = 724 cm(-1), respectively. These values correspond well to those (deltat = 4900 and B = 730 cm(-1)) of Co(II)-substituted "blue" copper proteins. The energy differences between S leads to M(II) charge transfer bands of Co(II)-Cu(II) couples were about 14,000 cm(-1) in both the proteins and the model complexes. The spectral results suggest that "blue" copper site has a pseudotetrahedral geometry and a deep absorption near 600 nm atributes to S leads to Cu(II) charge transfer.
对含巯基和咪唑的2:1肽 - 钴（II）配合物的电子性质进行了研究，并与钴（II）取代的“蓝色”铜蛋白的电子性质进行了比较。N - 巯基乙酰基 - L - 组氨酸和3 - 巯基丙酰基 - L - 组氨酸的钴（II）配合物的配体场参数分别为Δt = 4110和B = 756 cm⁻¹，以及Δt = 4120和B = 724 cm⁻¹。这些值与钴（II）取代的“蓝色”铜蛋白的值（Δt = 4900和B = 730 cm⁻¹）非常吻合。在蛋白质和模型配合物中，钴（II） - 铜（II）偶联的S→M（II）电荷转移带之间的能量差约为14,000 cm⁻¹。光谱结果表明，“蓝色”铜位点具有假四面体几何结构，600 nm附近的深吸收归因于S→Cu（II）电荷转移。
