School of Biosciences, Main Building, Cardiff University, Cardiff CF10 3AT, UK.
Chem Commun (Camb). 2012 Nov 7;48(86):10624-6. doi: 10.1039/c2cc34302a.
The biologically and nanotechnologically important heme protein cytochrome b(562) was reconstructed with zinc and copper porphyrins, leading to significant changes in the spectral, redox and electron transfer properties. The Cu form shifts the redox potential by +300 mV and exhibits high electron transfer, while the Zn form is redox inert.
生物和纳米技术上重要的血红素蛋白细胞色素 b(562) 被锌和铜卟啉重建，导致光谱、氧化还原和电子转移性质发生显著变化。Cu 形式将氧化还原电位移动+300 mV，并表现出高电子转移，而 Zn 形式则是氧化还原惰性的。
