Hartzell C R, Hansen R E, Beinert H
Proc Natl Acad Sci U S A. 1973 Sep;70(9):2477-81. doi: 10.1073/pnas.70.9.2477.
On the basis of oxidoreductive rapid kinetic and titration experiments with purified cytochrome c oxidase (EC 1.9.3.1), monitored by electron paramagnetic resonance (EPR) at 13 degrees K and by spectrophotometry at 100 degrees K, a new assignment of EPR signals is proposed. The bulk of both the low-spin (g = 3.0; 2.2; 1.5) and highspin (g = 6; 2) signals is attributed to the component with the properties of traditional cytochrome a. It is further proposed that the absorption band at 655 nm represents the most unambiguous manifestation of the a(3) component.
基于在13K下通过电子顺磁共振(EPR)以及在100K下通过分光光度法监测的、用纯化的细胞色素c氧化酶(EC 1.9.3.1)进行的氧化还原快速动力学和滴定实验,提出了EPR信号的新归属。低自旋(g = 3.0;2.2;1.5)和高自旋(g = 6;2)信号的大部分归因于具有传统细胞色素a特性的组分。进一步提出,655nm处的吸收带是a(3)组分最明确的表现。