Rasmussen C B, Bakovic M, Welinder K G, Dunford H B
Institute of Biochemical Genetics, University of Copenhagen, Denmark.
FEBS Lett. 1993 Apr 19;321(1):102-5. doi: 10.1016/0014-5793(93)80630-d.
The reaction of barley peroxidase BP 1 with H2O2 is markedly different from that of other peroxidases. Saturation kinetics and a strong pH dependence over the accessible pH range from 3.09 to 5.08 are observed. At pH 3.8, native BP 1 has maxima at 401, 498 and 635 nm, cpd 1 at 403 nm, and cpd II at 407 and 521 nm with a shoulder at 553 nm. Both cpds I and II appear to be incompletely formed. Isosbestic points between native BP 1 and cpd I occur at 365 and 416 nm, while an isosbestic point in the Soret region between cpd I and cpd II has been observed at 410 nm. Between cpd II and a not yet identified intermediate isosbestic points have been observed at 408, 455 and 526 nm.
大麦过氧化物酶BP 1与过氧化氢的反应与其他过氧化物酶明显不同。观察到饱和动力学以及在3.09至5.08的可及pH范围内对pH有很强的依赖性。在pH 3.8时，天然BP 1在401、498和635 nm处有最大值，化合物I在403 nm处，化合物II在407和521 nm处，在553 nm处有一个肩峰。化合物I和II似乎都未完全形成。天然BP 1与化合物I之间的等吸收点出现在365和416 nm处，而在化合物I和化合物II之间的索雷特区域观察到一个等吸收点在410 nm处。在化合物II与一个尚未鉴定的中间体之间，在408、455和526 nm处观察到等吸收点。
