Banci L, Bertini I, Pease E A, Tien M, Turano P
Department of Chemistry, University of Florence, Italy.
Biochemistry. 1992 Oct 20;31(41):10009-17. doi: 10.1021/bi00156a021.
1H NMR spectra at 200- and 600-MHz of manganese peroxidase from Phanerochaete chrysosporium and of its cyanide derivative are reported. The spectrum of the native protein is very similar to that of other peroxidases. The assignment of the spectrum of the cyanide derivative has been performed through 1D NOE, 2D NOESY, and COSY experiments. This protein is very similar to lignin peroxidase, the only meaningful difference being the shift of H delta 2 of the proximal histidine. The spectra of the cyanide derivative of these two proteins are compared with those of horseradish peroxidase and cytochrome c peroxidase. The shift pattern of the protons of the proximal histidine is discussed relative to the structural properties which affect the Fe3+/Fe2+ redox potential.
报道了黄孢原毛平革菌锰过氧化物酶及其氰化物衍生物在200兆赫和600兆赫下的1H核磁共振谱。天然蛋白质的谱图与其他过氧化物酶的谱图非常相似。氰化物衍生物的谱图归属是通过一维核Overhauser效应（1D NOE）、二维核Overhauser效应谱（2D NOESY）和化学位移相关谱（COSY）实验完成的。这种蛋白质与木质素过氧化物酶非常相似，唯一有意义的区别是近端组氨酸的Hδ2位移。将这两种蛋白质的氰化物衍生物的谱图与辣根过氧化物酶和细胞色素c过氧化物酶的谱图进行了比较。讨论了近端组氨酸质子的位移模式与影响Fe3+/Fe2+氧化还原电位的结构性质的关系。
