Lockart Molly M, Edwards Kyle C, Vincent John B, Pierce Brad S
Department of Chemistry, The University of Alabama, Tuscaloosa, AL 35487-0336, USA.
Polyhedron. 2021 Jul 15;203. doi: 10.1016/j.poly.2021.115224. Epub 2021 Apr 18.
An EPR signal for Mn(III) bound to the metal transport protein transferrin has been detected for the first time. The temperature dependence and simulations of the EPR signal are consistent with the Mn(III) centers being six-coordinate in an elongated tetragonal environment. Thus, the incorporation of Mn(III) within the Tf active site does not vastly alter the coordination number or active site geometry relative to native Fe(III)-Tf. This parallel mode EPR signal for Mn(III)-Tf could prove valuable for future studies aimed at determining the physiological relevance of Mn(III)-Tf.
首次检测到与金属转运蛋白转铁蛋白结合的Mn(III)的电子顺磁共振(EPR)信号。EPR信号的温度依赖性和模拟结果与Mn(III)中心在拉长的四方环境中为六配位一致。因此,相对于天然的Fe(III)-转铁蛋白,Mn(III)掺入转铁蛋白活性位点并不会极大地改变配位数或活性位点几何结构。Mn(III)-转铁蛋白的这种平行模式EPR信号可能对未来旨在确定Mn(III)-转铁蛋白生理相关性的研究具有重要价值。