Turner N, Ballard A L, Bray R C, Ferguson S
School of Chemistry and Molecular Sciences, University of Sussex, Brighton, U.K.
Biochem J. 1988 Jun 15;252(3):925-6. doi: 10.1042/bj2520925.
The molybdenum centre of respiratory nitrate reductase from Paracoccus denitrificans has been investigated by e.p.r. spectroscopy of Mo(V). In common with the centres of the analogous enzymes from Escherichia coli and Pseudomonas aeruginosa, it undergoes a pH- and anion-dependent transition between two different e.p.r. signal-giving species. Comparison of the relevant e.p.r. parameters extracted with the help of computer simulations reveals ligation of the metal in the active centres of the three enzymes to be identical.
利用钼(Ⅴ)的电子顺磁共振光谱对反硝化副球菌呼吸硝酸盐还原酶的钼中心进行了研究。与来自大肠杆菌和铜绿假单胞菌的类似酶的中心一样,它在两种不同的产生电子顺磁共振信号的物种之间经历了一个依赖于pH值和阴离子的转变。通过计算机模拟提取的相关电子顺磁共振参数的比较表明,这三种酶活性中心的金属配位是相同的。