Hawkes T R, Lowe D J, Smith B E
Biochem J. 1983 May 1;211(2):495-7. doi: 10.1042/bj2110495.
During turnover at 10 degrees C at pH 7.4 in the presence of ethylene, the MoFe protein of Klebsiella pneumoniae nitrogenase (Kp 1) exhibited an electron-paramagnetic-resonance signal with g-values at 2.12, 1.998 and 1.987. 57Fe isotopic substitution demonstrated that this signal arose from the Kp 1 FeMo-cofactor in an S = 1/2 spin state.
在10摄氏度、pH值为7.4且存在乙烯的条件下进行周转时,肺炎克雷伯氏菌固氮酶(Kp 1)的钼铁蛋白呈现出电子顺磁共振信号,其g值分别为2.12、1.998和1.987。57Fe同位素取代表明该信号源自处于S = 1/2自旋态的Kp 1铁钼辅因子。